ID H0A6L7_9PROT Unreviewed; 438 AA.
AC H0A6L7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:EHL96984.1};
GN ORFNames=HMPREF9946_04474 {ECO:0000313|EMBL:EHL96984.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL96984.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHL96984.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008954,
CC 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:EHL96984.1}.
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DR EMBL; AGEZ01000191; EHL96984.1; -; Genomic_DNA.
DR AlphaFoldDB; H0A6L7; -.
DR STRING; 1054213.HMPREF9946_04474; -.
DR PATRIC; fig|1054213.3.peg.4058; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_5; -.
DR OrthoDB; 9801834at2; -.
DR BioCyc; ABAC1054213:G1H32-4130-MONOMER; -.
DR Proteomes; UP000003292; Unassembled WGS sequence.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; 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; IPR004632; 4NH2But_aminotransferase_bac.
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 NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000003292};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 438 AA; 46551 MW; FAA56B2E43E80A13 CRC64;
MSVTSANKNQ ALQARREAAV PRGLGIQMPV FAAKAENAEI TDVEGKRYID FAGGIAVLNT
GHLHPKVKAA VTAQLENFSH TCIQVMPYEG YIRLAERLND IVPTRGPRKT IFVTTGAEAI
ENAVKIARAH TGRSGVIAFS GAFHGRTLMG MALTGKVVPY KVGFGAMPSD VYHLPFPVTY
HGKEVEQTLE ALEVMFRADV DPKRIAAMII EPVQGEGGFY IAQKELLQGI RRICDEHGIV
MIIDEVQTGF ARTGKMFAIE HSGVEPDIMT MAKSLAGGFP LSAVTGKAEI MDAPGPGGLG
GTYGGNPLSC AAANAVLDVI EEENLCARAD EIGELFVNRI KQLQDTNSLK GIIGDIRALG
AMVAMELVSG GNADSPDPDL AKALVKRAGE KGLVLLSCGV RGNVIRFLVP LTASDALINE
GMDILGECLR ECVADRAA
//
