(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHZ1_GEOS0

ID   A0A0F6BHZ1_GEOS0        Unreviewed;       401 AA.
AC   A0A0F6BHZ1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 26.
DE   SubName: Full=Cys/Met metabolism pyridoxal-phosphate-dependent protein {ECO:0000313|EMBL:ADP73042.1};
GN   OrderedLocusNames=GY4MC1_0190 {ECO:0000313|EMBL:ADP73042.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73042.1};
RN   [1] {ECO:0000313|EMBL:ADP73042.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73042.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CP002293; ADP73042.1; -; Genomic_DNA.
DR   RefSeq; WP_003247687.1; NC_014650.1.
DR   EnsemblBacteria; ADP73042; ADP73042; GY4MC1_0190.
DR   GeneID; 29237160; -.
DR   KEGG; gmc:GY4MC1_0190; -.
DR   KO; K01761; -.
DR   OMA; CYLYSRH; -.
DR   OrthoDB; 637281at2; -.
DR   BioCyc; GSP581103:G1GOQ-230-MONOMER; -.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHZ1.
DR   SWISS-2DPAGE; A0A0F6BHZ1.
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118}.
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   401 AA;  44324 MW;  AC019322CDA902D7 CRC64;
     MDKRDHREEM NLEGLRTETL VIHGDDWVID DRTVAPAIYY TATFRAHNSR EFAEMAGTPR
     HPRYYTRYGN PVHERVAKIM AELEGTETAL VTGSGMGAIA TTILTLVSAG DHVIAQTRHY
     MSTAKIMDEM LPRFGVEVTL VEQADINAFA EAIRPNTKLI MVETPANPTL VLTDLAAVVE
     LARPRGIIVV ADNTFASPIN QRPHDLGVDV VIHSATKYLG GHHDLTAGVI CTSKELAERI
     WQTHISIGSV LSPMDAWLLL RGLRTLPIRM ERINANALAL AEFLEEQPQV ERVYYPGLPS
     HPQHELAKRQ MRGFGAVIAF AIKGGYEETQ RFVSALKLPP NAVSLGGVDS LVVHTAAMWE
     GVMTEEQMKT AGIPANFVRF SVGLEHIDDL KADVWQALQV V
//

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