ID F7RRC6_9GAMM Unreviewed; 446 AA.
AC F7RRC6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Omega-amino acid--pyruvate aminotransferase {ECO:0000313|EMBL:EGM69123.1};
DE EC=2.6.1.18 {ECO:0000313|EMBL:EGM69123.1};
GN ORFNames=SOHN41_02931 {ECO:0000313|EMBL:EGM69123.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM69123.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM69123.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM69123.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGM69123.1}.
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DR EMBL; AFOZ01000037; EGM69123.1; -; Genomic_DNA.
DR RefSeq; WP_007650103.1; NZ_AFOZ01000037.1.
DR AlphaFoldDB; F7RRC6; -.
DR STRING; 327275.SOHN41_02931; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000002956; Unassembled WGS sequence.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF1; BETA-ALANINE--PYRUVATE AMINOTRANSFERASE; 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 Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EGM69123.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:EGM69123.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGM69123.1}.
SQ SEQUENCE 446 AA; 48471 MW; 0CF2FB43A5225E92 CRC64;
MADLQLNSLS NASSLEHFWM PFTANRQFKA NPRLLAKAEG MYYTDIDGNK VLDATAGLWC
CNAGHGRKEI SEAVSKQIQQ MDYAPSFQMG HPIAFELAER LTELSPEGLN KVFFTNSGSE
SVDTALKMAL CYHRANGQAS RTRFIGREMG YHGVGFGGIS VGGLSNNRKA FSGQLLQGVD
HLPHTLDIQN AAFTRGLSPF GAEKAEVLEQ LVTLHGAENI AAVIVEPMSG SAGVILPPQG
YLKRLREITK KHGILLIFDE VITAFGRVGA AFASQRWGVI PDMITTAKAI NNGAIPMGAV
FVQDFIHDTC MQGPIELIEF FHGYTYSGHP VAAAAALATL SIYENEQLFE RSFELERYFE
EAVHSLKGLP NVIDIRNTGL VAGIQLAPNA QGAGKRGYGV FEHCFRHGTL VRATGDIIAM
SPPLIVDKRE IDQMVNSLSD AINTVG
//
