ID   I4WZ93_9GAMM            Unreviewed;       444 AA.
AC   I4WZ93; M4NBF0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=4-aminobutyrate aminotransferase family protein {ECO:0000313|EMBL:AGG87960.1};
DE   Flags: Precursor;
GN   ORFNames=R2APBS1_0795 {ECO:0000313|EMBL:AGG87960.1};
OS   Rhodanobacter denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG87960.1, ECO:0000313|Proteomes:UP000011859};
RN   [1] {ECO:0000313|EMBL:AGG87960.1, ECO:0000313|Proteomes:UP000011859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2APBS1 {ECO:0000313|EMBL:AGG87960.1,
RC   ECO:0000313|Proteomes:UP000011859};
RG   US DOE Joint Genome Institute;
RA   Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Peters L., Pitluck S., Woyke T., Prakash O., Elkins J., Brown S.,
RA   Palumbo A., Hemme C., Zhou J., Watson D., Jardine P., Kostka J., Green S.;
RT   "Complete genome of Rhodanobacter sp. 2APBS1.";
RL   Submitted (APR-2012) 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|RuleBase:RU003560}.
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DR   EMBL; CP003470; AGG87960.1; -; Genomic_DNA.
DR   RefSeq; WP_007507154.1; NZ_CP088925.1.
DR   AlphaFoldDB; I4WZ93; -.
DR   STRING; 666685.R2APBS1_0795; -.
DR   KEGG; rhd:R2APBS1_0795; -.
DR   PATRIC; fig|666685.9.peg.126; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000011859; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:AGG87960.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AGG87960.1}.
SQ   SEQUENCE   444 AA;  47258 MW;  A8856EC06C96912E CRC64;
     MNATPNPNHI KTALPGPKAQ AMIARDAEVI SPSYPRDYPF VMSHGRGTEV WDVDGNRFLD
     FMAGIAVCAT GHAHPQVVKA VQDAAAKFLH ISSDYWHEEM VGLGERLAAV APLGEPAMSF
     ICQSGTEAVE GALKLARYVT GRPRFIGFLG GFHGRTFGSL SFTSSKYTQQ KGFSPTLAGV
     THVPYPNPYR PLFAGDDQGA AVLDYIRMLF QRSVPPSEVA AILIEPMQGE GGYLTPPDGF
     LAGLRALCDE HGILLIFDEV QSGIGRTGKM FACEHWGVAP DILTSAKGLG SGLPIGAVIA
     KKAIMAQWKR GAHGNTYGGN PVTCAAANAT LDLVRGGLMD NAATVGDHFM ARLRELQRDF
     PCIGEVRGKG LWIGMELIES DGKKTPATAL CEAVVQRAFH NGLLLLSCGT STVRFMPPLN
     VSVGEVDEAI ALLRASLDQA LAGA
//