ID C0W145_9ACTO Unreviewed; 276 AA.
AC C0W145;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Pyridoxal phosphate enzyme, YggS family {ECO:0000313|EMBL:EEH63534.1};
GN ORFNames=HMPREF0044_1135 {ECO:0000313|EMBL:EEH63534.1};
OS Gleimia coleocanis DSM 15436.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Gleimia.
OX NCBI_TaxID=525245 {ECO:0000313|EMBL:EEH63534.1, ECO:0000313|Proteomes:UP000010301};
RN [1] {ECO:0000313|EMBL:EEH63534.1, ECO:0000313|Proteomes:UP000010301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15436 {ECO:0000313|EMBL:EEH63534.1,
RC ECO:0000313|Proteomes:UP000010301};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR004848-1};
CC -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC YggS/PROSC family. {ECO:0000256|RuleBase:RU004514}.
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:EEH63534.1}.
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DR EMBL; ACFG01000032; EEH63534.1; -; Genomic_DNA.
DR AlphaFoldDB; C0W145; -.
DR STRING; 525245.HMPREF0044_1135; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_1_0_11; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000010301; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00635; PLPDE_III_YBL036c_like; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR029066; PLP-binding_barrel.
DR InterPro; IPR011078; PyrdxlP_homeostasis.
DR NCBIfam; TIGR00044; YggS family pyridoxal phosphate-dependent enzyme; 1.
DR PANTHER; PTHR10146; PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN; 1.
DR PANTHER; PTHR10146:SF14; PYRIDOXAL PHOSPHATE HOMEOSTASIS PROTEIN; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR004848-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010301};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..274
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 76
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 276 AA; 30301 MW; D22DBB96B351AA86 CRC64;
MVFRSAGTLY FIFSMPYHIT LPCFFHSFFF LLILVNMTPN FAHIYQNVSE VLDKIQACAE
MNHRHAAEIE LEIAIKTRSA TEALHAGLAL EASGRRALLA HNRVQEAQAT TPILRDGPLS
SFHSVLIGNL QRNKINAAVR VFDEIESVDS LALARALSQR LDPTEQLPIM LQVNTSRELS
KSGLVPEVAL ETALEIADLP GLLVTGFMTI GAHTTDQALI GKSFANLRAI RDEAIKHPSL
KKAINLSMGM SSDFELAIAE GSTRIRIGNA VFGPRL
//
