ID I0R2W7_9MICO Unreviewed; 441 AA.
AC I0R2W7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EIC92203.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:EIC92203.1};
GN ORFNames=IMCC13023_06820 {ECO:0000313|EMBL:EIC92203.1};
OS Candidatus Aquiluna sp. IMCC13023.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Aquiluna.
OX NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC92203.1, ECO:0000313|Proteomes:UP000054510};
RN [1] {ECO:0000313|Proteomes:UP000054510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX PubMed=22689238; DOI=10.1128/JB.00586-12;
RA Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT member of the Actinobacteria isolated from an arctic fjord.";
RL J. Bacteriol. 194:3550-3551(2012).
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:EIC92203.1}.
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DR EMBL; AJKR01000002; EIC92203.1; -; Genomic_DNA.
DR RefSeq; WP_007541296.1; NZ_AJKR01000002.1.
DR AlphaFoldDB; I0R2W7; -.
DR STRING; 1081644.IMCC13023_06820; -.
DR PATRIC; fig|1081644.3.peg.689; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000054510; 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 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:EIC92203.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000054510};
KW Transferase {ECO:0000313|EMBL:EIC92203.1}.
SQ SEQUENCE 441 AA; 46712 MW; 78F146A41B0F8119 CRC64;
MSLEQKRILN TPIPGPKSAE LQKRRTAVVS SGVGTMLPVF IERAHSAILE DVDGNQLIDM
GTGIGVVTIG HTNPGVVAAV QEQVAKLTHT LFTVAPYEKY VRAAELLAAH SPGSFPKKVA
FFNSGAEAVE NAVKIARRAT GRTEIAVFDH AYHGRTSLTM AMNFKAHPYA TGFGPLPGSI
HHAPMSYPFR DPEGMTGEQA AARTITYLEK RVGASQLAAV FIEPIQGEAG FIVPAPGFLK
TIDSWCKANG IVMVADEVQS GMARTGKWFA SQWEEGFDPD LVTVAKGIAG GMPLSGVVGR
AEIMDSAHAG GLGGTFGGSP TAVAAAVAVM EQLEQGNWLD RAQEIGAIIV ERLTEMMTMY
PVIGEVRGVG AMQAFELVMP GTLDPNQPAT DALLRHCHKN GVVVLNAGTY ANVVRLLPPL
SISDELLHEA LDVISEGLAT L
//
