ID A0A1M5EVR7_9BACT Unreviewed; 407 AA.
AC A0A1M5EVR7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924};
DE EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924};
DE AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|ARBA:ARBA00030587};
GN ORFNames=SAMN05444274_11041 {ECO:0000313|EMBL:SHF83132.1};
OS Mariniphaga anaerophila.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1484053 {ECO:0000313|EMBL:SHF83132.1, ECO:0000313|Proteomes:UP000184164};
RN [1] {ECO:0000313|EMBL:SHF83132.1, ECO:0000313|Proteomes:UP000184164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26910 {ECO:0000313|EMBL:SHF83132.1,
RC ECO:0000313|Proteomes:UP000184164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004998}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; FQUM01000010; SHF83132.1; -; Genomic_DNA.
DR RefSeq; WP_073003121.1; NZ_FQUM01000010.1.
DR AlphaFoldDB; A0A1M5EVR7; -.
DR STRING; 1484053.SAMN05444274_11041; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000184164; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004587; F:ornithine aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR010164; Orn_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01885; Orn_aminotrans; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW Iron {ECO:0000256|ARBA:ARBA00022714};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022714};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000184164}.
SQ SEQUENCE 407 AA; 45093 MW; A3874FFF747366A0 CRC64;
MVQLTTRDYI AKEDKFGAHN YHPIPVVLSK GEGVFVWDVE GKRYFDFLAA YSAVNQGHCH
PKIVKALTEQ AETLALTSRA FYNNTLGDWE EYMTQLFGYD KMLPMNSGAE ADETALKLIR
KWAYKVKGIP ENEAKIVVCD GNFHGRTITI ISMSSDPDAY SHYGPYTPGF VNIPYNDLQR
LEDELKDSNV AGFLVEPIQA EAGVYVPEDG YLKKAAELCK KHNVLFVADE VQTGLARTGK
MLACDHENVR PDILVLGKAL SGGMYPVSCV LADDEIMLTI KPGEHGSTYG GNPIAGRVAM
AALDVIQEEK LAENSLRLGE IFRNEMKAIP SEMIEIVRGK GLLNAVAIKP VNGKTAWDVC
VALKENGLLA KPTHEHIIRF TPPLVITEEQ LMEAIEIIKQ TFKEMGI
//
