ID A0A0S8BCS9_9PROT Unreviewed; 446 AA.
AC A0A0S8BCS9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMJ64_00650 {ECO:0000313|EMBL:KPK09384.1};
OS Betaproteobacteria bacterium SG8_39.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703390 {ECO:0000313|EMBL:KPK09384.1, ECO:0000313|Proteomes:UP000051483};
RN [1] {ECO:0000313|EMBL:KPK09384.1, ECO:0000313|Proteomes:UP000051483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_39 {ECO:0000313|EMBL:KPK09384.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK09384.1}.
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DR EMBL; LJTQ01000002; KPK09384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BCS9; -.
DR STRING; 1703390.AMJ64_00650; -.
DR Proteomes; UP000051483; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
SQ SEQUENCE 446 AA; 47993 MW; 05D7DE8BC919899E CRC64;
MTHVFHRDPR NRYPVAVRGE GAYLVDAQGK RYLDASGGAA VSCLGHSDRA VVEAIQRQLD
VLPYAHTSFF SNGPMEELAD VLVERSAGVF DKVYFVSGGS EAIEAALKLA RQYFVERGES
QRRYVIARAQ SYHGNTLGAL AVGGNPARRR QFEPLLIDAT HVSPCYAYRG LQPGENEAAY
GERLAQELER EIRRLDGDKV IAFVAETVSG ATLGAVPAVP GYFRRVRDVC DRYGVLLILD
EVMCGMGRCG SLFAYTQEEV VPDLVTVAKG LGAGYQPIGA VLSSKKVFDT IVGGSGFFQH
GHTYLGHAAA CAGALAVQRR LHEDGLLARV ASLGDALEAR LRAAFGDHPH VGDIRGRGLF
RGVELVAERG TKKPFDPTLR VHARLKQAAL AQGLMCYPMG GTVDGIRGDH VLLAPPFIVE
EAQLDELVAK LQAALKSTLS ALAAPA
//