Protein families database of alignments and HMMs   Aminotran_1_2

Figure 1: 2ay4 Aminotransferase Aromatic amino acid aminotransferase with 3-(p-tolyl)propionic acid Key: Domain Chain Start Residue End Residue Aminotran_1_2 A 85 408 Aminotran_1_2 B 85 408 The Swissprot/PDB mapping was provided by MSD 1aam1aaw1ahe1ahf1ahg1ahx1ahy1aia1aib1aic1ajr1ajs1aka1akb1akc1ama1amq1amr1ams1arg1arh1ari1ars1art1asa1asb1asc1asd1ase1asf1asg1asl1asm1asn1ay41ay51ay81b4x1b8g1bjw1bkg1bqa1bqd1bs01bw01c7n1c7o1c9c1cq61cq71cq81czc1cze1d2f1dj91dje1dju1fc41fg31fg71g4v1g4x1g7w1g7x1gc31gc41gck1gd91gew1gex1iax1iay1iji1ivr1ix61ix71ix81j321lc51lc71lc81lkc1m4n1m7y1map1maq1o4s1oxo1oxp1qir1qis1qit1spa1tar1tas1tat1yaa1yoo2aat2ay12ay22ay32ay52ay62ay72ay82ay92cst3aat3tat5eaa7aat8aat9aat

Accession number: PF00155 Previous identifiers: aminotran_1; aminotran_1_2; Aminotransferase class I and II INTERPRO description (entry IPR004839) Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped MEDLINE:91115885 into class I and class II. This entry includes both subfamilies. QuickGO FUNCTION : transaminase activity (GO:0008483) PROCESS : biosynthesis (GO:0009058)

For additional annotation, see the PROSITE document PDOC00098 [Expasy|SRS-UK|SRS-USA]

Alignment	Domain organisation
Seed (48)  Full (1715) Format Coloured alignment Plain Pfam format Plain Stockholm format Fasta format (with gaps) MSF format Belvu (unix only) Belvu (old version unix only) Jalview (Java) Further alignment options here Help relating to Pfam alignments here	Seed (48)  Full (1715) Context (4) As a Graphic As a Tree Zoom pixels/aa. Bootstrap tree To find out about the NIFAS tree-viewer, click here
Species Distribution	Phylogenetic tree
View alignments & domain organisation by species Tree depth : Show all levels 1 level 2 levels 3 levels 4 levels 5 levels	Seed (48)  Full (1715) The trees were generated using Quicktree To find out more about ATV phylogenetic tree-viewer click here

Database References
PDB You can find out how to set up Rasmol here	1aam ; 92; 408; 1aaw ; 92; 408; 1ahe A; 85; 409; 1ahe B; 85; 409; 1ahf A; 85; 409; 1ahf B; 85; 409; 1ahg A; 85; 409; 1ahg B; 85; 409; 1ahx A; 85; 409; 1ahx B; 85; 409; 1ahy A; 85; 409; 1ahy B; 85; 409; 1aia A; 85; 409; 1aia B; 85; 409; 1aib A; 85; 409; 1aib B; 85; 409; 1aic A; 85; 409; 1aic B; 85; 409; 1ajr A; 85; 408; 1ajr B; 85; 408; 1ajs A; 85; 408; 1ajs B; 85; 408; 1aka A; 85; 409; 1aka B; 85; 409; 1akb A; 85; 409; 1akc A; 85; 409; 1ama ; 85; 409; 1amq ; 85; 409; 1amr ; 85; 409; 1ams ; 85; 409; 1arg A; 85; 409; 1arg B; 85; 409; 1arh A; 85; 409; 1arh B; 85; 409; 1ari A; 85; 409; 1ari B; 85; 409; 1ars ; 85; 409; 1art ; 85; 409; 1asa ; 92; 408; 1asb ; 92; 408; 1asc ; 92; 408; 1asd ; 92; 408; 1ase ; 92; 408; 1asf ; 92; 408; 1asg ; 92; 408; 1asl A; 85; 409; 1asl B; 85; 409; 1asm A; 85; 409; 1asm B; 85; 409; 1asn A; 85; 409; 1asn B; 85; 409; 1ay4 A; 85; 408; 1ay4 B; 85; 408; 1ay5 A; 85; 408; 1ay5 B; 85; 408; 1ay8 A; 85; 408; 1ay8 B; 85; 408; 1b4x A; 85; 409; 1b8g A; 97; 429; 1b8g B; 97; 429; 1bjw A; 79; 382; 1bjw B; 79; 382; 1bkg A; 79; 382; 1bkg B; 79; 382; 1bkg C; 79; 382; 1bkg D; 79; 382; 1bqa A; 85; 409; 1bqa B; 85; 409; 1bqd A; 85; 409; 1bqd B; 85; 409; 1bs0 A; 71; 381; 1bw0 A; 86; 410; 1bw0 B; 86; 410; 1c7n A; 77; 206; 1c7n B; 77; 206; 1c7n C; 77; 206; 1c7n D; 77; 206; 1c7n E; 77; 206; 1c7n F; 77; 206; 1c7n G; 77; 206; 1c7n H; 77; 206; 1c7o A; 77; 206; 1c7o B; 77; 206; 1c7o C; 77; 206; 1c7o D; 77; 206; 1c7o E; 77; 206; 1c7o F; 77; 206; 1c7o G; 77; 206; 1c7o H; 77; 206; 1c9c A; 85; 409; 1cq6 A; 85; 409; 1cq7 A; 85; 409; 1cq8 A; 85; 409; 1czc A; 85; 409; 1cze A; 85; 409; 1d2f A; 74; 383; 1d2f B; 74; 383; 1dj9 A; 71; 381; 1dje A; 71; 381; 1dju A; 74; 383; 1dju B; 74; 383; 1fc4 A; 74; 388; 1fc4 B; 74; 388; 1fg3 A; 69; 355; 1fg7 A; 69; 355; 1g4v A; 85; 409; 1g4x A; 85; 409; 1g7w A; 85; 409; 1g7x A; 85; 409; 1gc3 A; 79; 382; 1gc3 B; 579; 882; 1gc3 C; 1079; 1382; 1gc3 D; 1579; 1882; 1gc3 E; 2079; 2382; 1gc3 F; 2579; 2882; 1gc3 G; 3079; 3382; 1gc3 H; 3579; 3882; 1gc4 A; 79; 382; 1gc4 B; 579; 882; 1gc4 C; 1079; 1382; 1gc4 D; 1579; 1882; 1gck A; 79; 382; 1gck B; 579; 882; 1gd9 A; 74; 383; 1gd9 B; 574; 883; 1gew A; 69; 351; 1gex A; 69; 351; 1iax A; 104; 434; 1iax B; 104; 434; 1iay A; 104; 434; 1iji A; 69; 355; 1ivr A; 82; 400; 1ix6 A; 85; 409; 1ix7 A; 85; 409; 1ix8 A; 85; 409; 1j32 A; 78; 384; 1j32 B; 78; 384; 1lc5 A; 65; 357; 1lc7 A; 65; 357; 1lc8 A; 65; 357; 1lkc A; 65; 357; 1m4n A; 97; 429; 1m7y A; 97; 429; 1map ; 85; 409; 1maq ; 85; 409; 1o4s A; 77; 374; 1o4s B; 77; 374; 1oxo A; 85; 409; 1oxo B; 85; 409; 1oxp ; 85; 409; 1qir A; 85; 409; 1qis A; 85; 409; 1qit A; 85; 409; 1spa ; 85; 409; 1tar A; 85; 409; 1tar B; 85; 409; 1tas A; 85; 409; 1tas B; 85; 409; 1tat A; 85; 409; 1tat B; 85; 409; 1yaa A; 85; 408; 1yaa B; 85; 408; 1yaa C; 85; 408; 1yaa D; 85; 408; 1yoo ; 85; 409; 2aat ; 92; 408; 2ay1 A; 85; 408; 2ay1 B; 85; 408; 2ay2 A; 85; 408; 2ay2 B; 85; 408; 2ay3 A; 85; 408; 2ay3 B; 85; 408; 2ay4 A; 85; 408; 2ay4 B; 85; 408; 2ay5 A; 85; 408; 2ay5 B; 85; 408; 2ay6 A; 85; 408; 2ay6 B; 85; 408; 2ay7 A; 85; 408; 2ay7 B; 85; 408; 2ay8 A; 85; 408; 2ay8 B; 85; 408; 2ay9 A; 85; 408; 2ay9 B; 85; 408; 2cst A; 85; 408; 2cst B; 85; 408; 3aat ; 85; 409; 3tat A; 85; 408; 3tat B; 85; 408; 3tat C; 85; 408; 3tat D; 85; 408; 3tat E; 85; 408; 3tat F; 85; 408; 5eaa A; 85; 409; 7aat A; 85; 409; 7aat B; 85; 409; 8aat A; 85; 409; 8aat B; 85; 409; 9aat A; 85; 409; 9aat B; 85; 409;
PROSITE 1-aminocyclopropane-1-carboxylate synthase signature	PDOC00518 [Expasy|SRS-UK|SRS-USA]
PRINTS	PR00753
PROSITE	PDOC00098 [Expasy|SRS-UK|SRS-USA]
PRINTS aspartate aminotransferase signature	PR00799
COGS	COG0079 COG0156 COG0436 COG1168 COG1448
HOMSTRAD	aat
PFAMB	PB000347 PB003487 PB004037 PB021045 PB036387 PB041649 PB044383 PB051518 PB055703 PB059775 PB066709 PB068442 PB074045 PB099779 PB104904 PB105989 PB106250 PB108010 PB108157 PB108169 PB108171 PB108175 PB108179 PB108186 PB108371 PB108623
SYSTERS	Aminotran_1_2
PANDIT	Aminotran_1_2

Literature References 1. Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS; Acta Crystallogr D Biol Crystallogr 1999;55:1474-1477. 2. Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K; Biochemistry 1999;38:2413-2424.

Pfam specific information Author of entry Sonnhammer ELL, Griffiths-Jones SR Type definition Domain Alignment method of seed Clustalw Source of seed members Prosite Average Length 290.0 Average %id 17 Average Coverage 70.88% HMMER build information   Pfam_ls  [Download HMM] Pfam_fs  [Download HMM] Gathering cutoff 5.0 5.0; 16.4 16.4 Trusted cutoff 5.3 5.3; 16.5 16.5 Noise cutoff 4.4 4.4; 16.3 16.3 Build method of HMM hmmbuild -F HMM_ls SEED hmmcalibrate --seed 0 HMM_ls hmmbuild -f -F HMM_fs SEED hmmcalibrate --seed 0 HMM_fs

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