ID C0Z928_BREBN Unreviewed; 414 AA.
AC C0Z928;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Purine catabolism protein {ECO:0000313|EMBL:BAH42498.1};
GN Name=pucG {ECO:0000313|EMBL:BAH42498.1};
GN OrderedLocusNames=BBR47_15210 {ECO:0000313|EMBL:BAH42498.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH42498.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH42498.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; AP008955; BAH42498.1; -; Genomic_DNA.
DR RefSeq; WP_012685247.1; NC_012491.1.
DR AlphaFoldDB; C0Z928; -.
DR STRING; 358681.BBR47_15210; -.
DR KEGG; bbe:BBR47_15210; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_0_0_9; -.
DR Proteomes; UP000001877; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001877}.
FT DOMAIN 38..351
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 414 AA; 45725 MW; B54EE20D637D4B21 CRC64;
MCAYKELTTS QRTIMTPGPV EAEPSVLRVM GSPILGQFDP EFTDIMNETM EMLRKLFQTS
NHWAFPIDGT SRAGIEAVLC SIIEPGDRVL VPIYGRFGHL LTEISERYGA DVITMETRWG
SVFEPKDVIA EIERVQPKIV AMVHGETSTG CVQPLKEIGE ACRRMDVLFV VDAVASIGGT
EVKVDDWYID ACIGGTQKCL SVPSGMAPIT FNSRIEELLL QRKKIERGLA DPSAPKSAQT
RTIRSNYFDL SQLMDYWGPA RLNHHTEATT MLYALREGVR IALTEGLEAR FARHRLHEQA
LVAGVLAMGL QLYGDPACKL PVVTCIKIPD GLDGESVRAM LLEDFHIEIA SSFGPLKGTI
WRIGTMGYSC RKKNILHVLG ALEAVLIRHG ARVHAGRAVQ AALDIYDQEK GQNS
//