ID A0A1F5C5G9_9BACT Unreviewed; 457 AA.
AC A0A1F5C5G9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=4-aminobutyrate aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2V45_08565 {ECO:0000313|EMBL:OGD38091.1};
OS Candidatus Aminicenantes bacterium RBG_19FT_COMBO_58_17.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797275 {ECO:0000313|EMBL:OGD38091.1, ECO:0000313|Proteomes:UP000178644};
RN [1] {ECO:0000313|EMBL:OGD38091.1, ECO:0000313|Proteomes:UP000178644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD38091.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MEYD01000084; OGD38091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5C5G9; -.
DR STRING; 1797275.A2V45_08565; -.
DR Proteomes; UP000178644; 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; 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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
SQ SEQUENCE 457 AA; 50341 MW; 25185A41D37F752B CRC64;
MEQSTLGPKS KAILRQTLEH ESIGHLSFGL FPCPPVVDRA KGAKMWDADG KEYIDFHSGF
SVNVLGHCHP EVNEAVKVQL DKLQQFAELP CQVRAEFSEK FLGLLPWDYP KKCQITVTGG
EAVEVAMKVS RWYTGKPIIM TQYGDYHGRT AGAMALTSKA SMLAYHYPVL PGDSGIFRFH
FAYCYRCPFG YSYPGCDIQC VKAVEYLFES KETWLNNPGA GITNVAAMII EPFQSSAGYI
ISPPEYLQGL KAICDRYGIL FVSDEVQSGM GRTGKTWAIE HSGVTPDLIT AAKSLSNGLP
ISVCAGRKEI LDSWGPTAHS TTYCGYPVAC AGGLKVLEIF ERDKIVEGVA KKGEYLAEGL
RSLQRSHPIV GHFDCKGLYA AIELVRDRRT KAPAGPETGY VLTSCLDEGL IFIASGYFYN
RLAFAPPFVI SKDEIDHGLA ILDRVLSRAE QKFDIKP
//
