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Database: UniProt
Entry: A0A1N7LPB4_9RHOB
LinkDB: A0A1N7LPB4_9RHOB
Original site: A0A1N7LPB4_9RHOB 
ID   A0A1N7LPB4_9RHOB        Unreviewed;       420 AA.
AC   A0A1N7LPB4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:SIS75668.1};
GN   ORFNames=SAMN05421580_104213 {ECO:0000313|EMBL:SIS75668.1};
OS   Rhodobacter aestuarii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=453582 {ECO:0000313|EMBL:SIS75668.1, ECO:0000313|Proteomes:UP000186221};
RN   [1] {ECO:0000313|Proteomes:UP000186221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19945 {ECO:0000313|Proteomes:UP000186221};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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; FTOG01000004; SIS75668.1; -; Genomic_DNA.
DR   RefSeq; WP_076484463.1; NZ_QAXT01000005.1.
DR   AlphaFoldDB; A0A1N7LPB4; -.
DR   STRING; 453582.SAMN05421580_104213; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000186221; Unassembled WGS sequence.
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; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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:SIS75668.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186221};
KW   Transferase {ECO:0000313|EMBL:SIS75668.1}.
SQ   SEQUENCE   420 AA;  44973 MW;  3846E0537B606F28 CRC64;
     MTDLIARREA LLGPNVPTFY DDPVHIVRGE GVWLYDAKGR RYLDCYNNVA HLGHCHPRVV
     EAIAHQAAQL NTHSRYLHEG ILDYGERLVA KFDHGLSQML MTCTGSEAND VALRMAQAVT
     GKTGLIATDN TYHGNTTAVA HLSTRRPPIG GYPPHIRRVP APDSLAPLGG SPKAQAKAFA
     ANVAQAIEEL EQAGHGFAGL MLCPIFANEG MPGLAPGFLD ATVNVVKRAG GLILCDEVQP
     GFGRLGSHWW GHELLGFAPD LVTLGKPMGN GHPVAAVVAR PDVMAAFRNA FGYFNTFAGN
     PVSCAAANAV LDVIEDEGLV ENAEAVGAYA LGLLLELRHP LIADVRGLGL FFAIEFARDG
     LPDGAFCGRV VEAAKDRGIL LGRVGRAQHI LKMRPPLPFS RENAQMLATT LKDILQEMPA
//
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