ID A0A0S8B3C8_9CHLR Unreviewed; 441 AA.
AC A0A0S8B3C8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KPK06120.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KPK06120.1};
GN ORFNames=AMJ56_14945 {ECO:0000313|EMBL:KPK06120.1};
OS Anaerolineae bacterium SG8_19.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703386 {ECO:0000313|EMBL:KPK06120.1, ECO:0000313|Proteomes:UP000050892};
RN [1] {ECO:0000313|EMBL:KPK06120.1, ECO:0000313|Proteomes:UP000050892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_19 {ECO:0000313|EMBL:KPK06120.1};
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 -!- 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:KPK06120.1}.
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; LJNN01000214; KPK06120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8B3C8; -.
DR Proteomes; UP000050892; Unassembled WGS sequence.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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 Aminotransferase {ECO:0000313|EMBL:KPK06120.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KPK06120.1}.
SQ SEQUENCE 441 AA; 48365 MW; CD23BB2410097830 CRC64;
MNTKLSGAGP LGQTIIKRDE ASLSPSYKRE YALVIDQAQG SEVWDADGRR YIDFMAGVAV
LNVGHRHPVV VEKVKEQMER FWHICLSDFY YPNAVELAEK LQEIAPMDQT LVYFGNTGTE
AVEAAIKLAM YATGRPKFIG FMGAFHGRTL GSLSFTASKA VQRANYLEGV NVHHVPFPNP
YRPLLAGHRE DNYGDIVINY IENEVFRTFL SPNDVAAVLI EPIQGEGGYV VPAPGFFQRL
RQLCDQHGIL LIVDEIQSGI ARTGKWWAVE HEGIEPDIIC FAKSIGSGMP IGGIIARSEL
MTWGPGAHGS TFGGNPLAAA AAIATLKVIE EEGLMEQATE SGQFILDALA EMQVRHPSIG
DIRGRGLMIG LELVKDKQTK ERAPELRSQI IQQAFESGLL LLSCGTNSIR FTPALNISQS
LVNEGLQIFE AVLTDAEREL L
//
