ID X0IRS5_FUSOX Unreviewed; 502 AA.
AC X0IRS5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=4-aminobutyrate aminotransferase {ECO:0000256|ARBA:ARBA00018543};
DE EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE AltName: Full=GABA aminotransferase {ECO:0000256|ARBA:ARBA00031787};
DE AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000256|ARBA:ARBA00030204};
GN ORFNames=FOPG_02153 {ECO:0000313|EMBL:EXL86670.1};
OS Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL86670.1};
RN [1] {ECO:0000313|EMBL:EXL86670.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54008 {ECO:0000313|EMBL:EXL86670.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW808.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXL86670.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=54008 {ECO:0000313|EMBL:EXL86670.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Annotation of Fusarium oxysporum PHW808.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00000442};
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; JH658806; EXL86669.1; -; Genomic_DNA.
DR EMBL; JH658806; EXL86670.1; -; Genomic_DNA.
DR HOGENOM; CLU_016922_12_0_1; -.
DR Proteomes; UP000030676; 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; IPR004631; 4NH2But_aminotransferase_euk.
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; TIGR00699; GABAtrns_euk; 1.
DR PANTHER; PTHR43206:SF1; 4-AMINOBUTYRATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43206; AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
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 ECO:0000313|EMBL:EXL86670.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EXL86670.1}.
SQ SEQUENCE 502 AA; 55136 MW; E59FA43232111E1E CRC64;
MSAFRAGMAA RPAVQAARAA ACRSFATSRS MRMAAASEKT FFAGEPEAPT VKTAIPGPKT
KSHMDELTKV FDTRSANMLV DYTKSKGNYI ADPDGNVLLD VFAQIASIAV GYNNPALLKA
ASSPEMVNAI VNRPALGAFP SHDWADLLKS SLLTVAPKGL DNVFTAMAGS DANETAYKAA
FMWRRQQERG GPEVDFSTKE LDSAMNNHAP GSPDLSILSF KTGFHGRLFG SLSTTRSKAI
HKVDIPAFDW PQATFPKLKY PLEENVEENK KIEQASLDEV EHLIKSWHLP PCAVVVEPVQ
SEGGDNHASP DFFRKLRALT KKHNILLIVD EVQTGIGATG KFWAHEHWNL ETPPDIVTFS
KKAQAAGFYY GDPAIRPNKP YRQFNTWMGD PARAILFKAI VDEINKNDLV NHTARVGDRL
FKDLESLSKK YPGQIENLRG KGQGTFIAFD SPKRDQFLAE AKKLGVNIGG SGASAVRLRP
MLIFQQKHAD ILVDTIEKIV KQ
//
