(data stored in SCRATCH zone)

SWISSPROT: D6ZCM3_SEGRD

ID   D6ZCM3_SEGRD            Unreviewed;       125 AA.
AC   D6ZCM3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 48.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976554};
DE            Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01021};
DE            EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976537};
GN   Name=hisI {ECO:0000256|HAMAP-Rule:MF_01021};
GN   OrderedLocusNames=Srot_0583 {ECO:0000313|EMBL:ADG97065.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97065.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG97065.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC       phosphoribosyl-AMP. {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00976573}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-
CC         beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC         ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC         Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC         ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01021, ECO:0000256|SAAS:SAAS01115149};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976563}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00976534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021,
CC       ECO:0000256|SAAS:SAAS00976539}.
CC   -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP-
CC       Rule:MF_01021, ECO:0000256|SAAS:SAAS00976567}.
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DR   EMBL; CP001958; ADG97065.1; -; Genomic_DNA.
DR   RefSeq; WP_013137521.1; NC_014168.1.
DR   STRING; 640132.Srot_0583; -.
DR   EnsemblBacteria; ADG97065; ADG97065; Srot_0583.
DR   KEGG; srt:Srot_0583; -.
DR   eggNOG; ENOG4105K8F; Bacteria.
DR   eggNOG; COG0139; LUCA.
DR   HOGENOM; HOG000277504; -.
DR   KO; K01496; -.
DR   OMA; TGYRSCF; -.
DR   OrthoDB; 1842189at2; -.
DR   BioCyc; SROT640132:G1GLH-589-MONOMER; -.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.20.400; -; 1.
DR   HAMAP; MF_01021; HisI; 1.
DR   InterPro; IPR026660; PRA-CH.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR   InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR   Pfam; PF01502; PRA-CH; 1.
DR   ProDom; PD002610; PRA_CycHdrlase; 1.
DR   SUPFAM; SSF141734; SSF141734; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZCM3.
DR   SWISS-2DPAGE; D6ZCM3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976560};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976532};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976556};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976548, ECO:0000313|EMBL:ADG97065.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976550};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021,
KW   ECO:0000256|SAAS:SAAS00976576};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976542}.
FT   DOMAIN       43    115       PRA-CH. {ECO:0000259|Pfam:PF01502}.
FT   METAL        90     90       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL        91     91       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01021}.
FT   METAL        92     92       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL        94     94       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01021}.
FT   METAL       107    107       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01021}.
FT   METAL       114    114       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01021}.
SQ   SEQUENCE   125 AA;  13404 MW;  E39CB9FC57D302C7 CRC64;
     MSESPAPGPA PALDPAVAAR LKRNADGLVA AVVQRRGTGE VLMMAWMDDE ALARTLTSRR
     GTYFSRSRGR LWVKGETSGN TQEVVEVRLD CDGDTVLVVV DQTGPSCHTG TSTCFDSDVL
     LRPKV
//

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