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Database: UniProt
Entry: A0A166RLZ8_9RHOB
LinkDB: A0A166RLZ8_9RHOB
Original site: A0A166RLZ8_9RHOB 
ID   A0A166RLZ8_9RHOB        Unreviewed;       476 AA.
AC   A0A166RLZ8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE   Flags: Fragment;
GN   ORFNames=A3721_06640 {ECO:0000313|EMBL:KZX98276.1};
OS   Sulfitobacter sp. HI0023.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZX98276.1, ECO:0000313|Proteomes:UP000077323};
RN   [1] {ECO:0000313|EMBL:KZX98276.1, ECO:0000313|Proteomes:UP000077323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0023 {ECO:0000313|EMBL:KZX98276.1,
RC   ECO:0000313|Proteomes:UP000077323};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC         EC=5.3.1.9; Evidence={ECO:0000256|ARBA:ARBA00029321,
CC         ECO:0000256|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|RuleBase:RU000612}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|RuleBase:RU000612}.
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:KZX98276.1}.
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DR   EMBL; LWEQ01000374; KZX98276.1; -; Genomic_DNA.
DR   RefSeq; WP_068101643.1; NZ_LWEQ01000374.1.
DR   AlphaFoldDB; A0A166RLZ8; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000077323; Unassembled WGS sequence.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05015; SIS_PGI_1; 1.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035476; SIS_PGI_1.
DR   InterPro; IPR035482; SIS_PGI_2.
DR   PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW   ECO:0000256|RuleBase:RU000612};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077323}.
FT   NON_TER         476
FT                   /evidence="ECO:0000313|EMBL:KZX98276.1"
SQ   SEQUENCE   476 AA;  51899 MW;  D6F4F231BFA45A11 CRC64;
     MTNTAQIWQA LDEKAAAIAD RSLLSFFDTP GRAAAFSVRT EDMLLDYSKT DIDQQARQLL
     LDLADMTGVE ARREAMFSGQ SINETEGRAV LHTALRNLDG DAVEVEGEDV MPGVHRTLAA
     MRDFAETIRS GDITDVVNIG IGGSDLGPAM AVAALAPYHD GPRCHFVSNV DGAHIADVLR
     TLDPRRTLVI VASKTFTTIE TMTNARTARA WMTDGGGDPA AQFAALSSAT DKTESFGIPP
     EHVFGFENWV GGRYSVWGPI GLSLMIAIGP RAFDAFLRGG QAMDRHFRAA ALQENMPVLL
     ALVGIWHNQI RGRATRAVLP YDQRLSLLPA YLQQLEMESN GKSTRMDGSV GPRHTGPIVW
     GAAGTNGQHA FYQLLHQGTR IVPCEFLVAA QGHEPELEHH HTLLLANCLA QSEALMRGRS
     LPEARALMAE AGHEGEELER QAAHRVFPGN RPSTTLIYPL LDPFTLGRII ALYEHR
//
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