ID R5BZ83_9FIRM Unreviewed; 464 AA.
AC R5BZ83;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=4-aminobutyrate aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN499_02794 {ECO:0000313|EMBL:CCX59534.1};
OS Blautia hydrogenotrophica CAG:147.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1263061 {ECO:0000313|EMBL:CCX59534.1, ECO:0000313|Proteomes:UP000018163};
RN [1] {ECO:0000313|EMBL:CCX59534.1, ECO:0000313|Proteomes:UP000018163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:147 {ECO:0000313|Proteomes:UP000018163};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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}.
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:CCX59534.1}.
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DR EMBL; CAWR010000191; CCX59534.1; -; Genomic_DNA.
DR AlphaFoldDB; R5BZ83; -.
DR Proteomes; UP000018163; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; 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; 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; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018163}.
SQ SEQUENCE 464 AA; 51146 MW; DE3E3EF88DFD27B1 CRC64;
MGRQFSLEPR NVKLVDTKYR KIKTQIPNPE STSLVRRMRT CEPVSMSGQP VIVWDAAKGC
QVYDKSGNCW IDFSSGVVVT NAGHCNPEVQ KAILETVEHG LLHSYCFPTE QRGRLEMRIS
ELVPIPDNRV FLLTTGAEST ECAIKLARTY GALKSDTKIK IVTFEDAFHG RTMGSQQAGG
SPAGKAWIKN LDKDILQVPF PNAFKYQWAD EKDEDYSDDR CFAMFLKSLE DAGVNPKEIA
GVMTETFQGG WCQLMPKGFV QRLRKFCTEH DILLIFDEVQ AGFGRTGKMF GFLHAEVTPD
LICCGKGISS SLPLSCVVGR SDVMNLYGPN QMTSTHTGNP VCSAAALASM NYIVGHGLVE
NAAKMGEVCE KKLREIQKRY PDHIGFVCGV GLAWAVIFTK PGTKEMDCET ACDVVERSFE
KGLLFFAPVG SGATIKVCPP LMISEEILRE GLDTFEEAVS EVLG
//
