(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   08-MAY-2019, entry version 20.
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.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73042.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73042.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73042.1,
RC   ECO:0000313|Proteomes:UP000002034};
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.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
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; SMTHSVV; -.
DR   OrthoDB; 637281at2; -.
DR   BioCyc; GSP581103:G1GOQ-230-MONOMER; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; 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   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118}.
FT   MOD_RES     217    217       N6-(pyridoxal phosphate)lysine.
FT                                {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
//

If you have problems or comments...

PBIL Back to PBIL home page