ID Q094Z5_STIAD Unreviewed; 423 AA.
AC Q094Z5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:EAU67305.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:EAU67305.1};
GN Name=gabT {ECO:0000313|EMBL:EAU67305.1};
GN OrderedLocusNames=STAUR_3537 {ECO:0000313|EMBL:ADO71327.1};
GN ORFNames=STIAU_4930 {ECO:0000313|EMBL:EAU67305.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU67305.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU67305.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU67305.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO71327.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO71327.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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}.
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DR EMBL; CP002271; ADO71327.1; -; Genomic_DNA.
DR EMBL; AAMD01000036; EAU67305.1; -; Genomic_DNA.
DR RefSeq; WP_002613184.1; NZ_AAMD01000036.1.
DR STRING; 378806.STAUR_3537; -.
DR KEGG; sur:STAUR_3537; -.
DR PATRIC; fig|378806.16.peg.6496; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_7; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; 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 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:0000313|EMBL:EAU67305.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EAU67305.1}.
SQ SEQUENCE 423 AA; 45540 MW; 67007F9A46DDA26B CRC64;
MSDNNVNLLR RKDAATPRGV GVMAPFFVSR AENSELWDVE GRRFIDFAGG IAVLNTGHRH
PRVVEAVKAQ LDAFTHSAYQ IVPYEAYVRL AERLNRLTPG AFAKKTTFFS TGAEAIENAV
KIARSATGRS GIIAFSGGFH GRTMMGLALT GKVVPYKAGF GPFPPEVYHV PFPIALHGIS
VEDTLRAFQN LFKADIEPKR VAAILIEPVQ GEGGFYVAPP ELMRSLRKLC DEHGILLIAD
EVQTGFARTG KWFAMDHHDV HPDLIVTAKS LAGGFPLSAV TGRAEVMDAP EPGGLGGTYA
GNPLAIAAAN AVLDIIEDEG LVKRANELGD VLRIKLEGLK AKVPQMAEVR GLGAMLAVEF
CQPGGHTPDT EFTKVVKARA LEKGLMLLTC GVYSNVIRFL FPLTVPEPVF KEGLSILESA
LTG
//
