ID A0A1F5CNB5_9ARCH Unreviewed; 447 AA.
AC A0A1F5CNB5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:OGD44317.1};
GN ORFNames=A3K69_01105 {ECO:0000313|EMBL:OGD44317.1};
OS Candidatus Bathyarchaeota archaeon RBG_16_57_9.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1797382 {ECO:0000313|EMBL:OGD44317.1, ECO:0000313|Proteomes:UP000177200};
RN [1] {ECO:0000313|EMBL:OGD44317.1, ECO:0000313|Proteomes:UP000177200}
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:OGD44317.1}.
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DR EMBL; MEZI01000070; OGD44317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5CNB5; -.
DR Proteomes; UP000177200; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 Aminotransferase {ECO:0000313|EMBL:OGD44317.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:OGD44317.1}.
SQ SEQUENCE 447 AA; 49701 MW; EE5A2522C89EF18B CRC64;
MSGLSYPKIK ITPPGPKAKK VVERDAAVIS PSFGRAYPLV IERGEGNIVV DVDGNEFIDM
NAGLAVCSVG HSHPKVVKAI KDQVDRFIHY SYTDFFYDGY VNLGEVLHDL VPGKHKKKFF
YGNSGAEAIE AAMKVSRWHS QRQGMLAYIG SFHGRTMGAV SLTASKPYQR RRFSPLVPGV
EHIFYPYCYR CPFHLECPSC GHYCVDYIDE YLFQKYVPAE EVSMLLAEPI QGEGGYVVPP
DGYFKKLKKL LDENGILLAM DEVQSGIGRT GKWFAIEHWG VVPDIVCMAK GIAAGMPLGV
MASRADIQDW TPGSHASTFG GNPVSCAAAL AVIEVIKSER LLENAQREGA YIKKRLEEMM
ETHPMMGDVR GKGLMVGVEL VKDRETKEYA KQETEDVMME CFRQGLAIVN CGVNVIRWMP
PLTITRDLVD PSLEIFEKSL SKVEKGK
//
