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Bifunctional PGK/TIM (EC 2.7.2.3) (EC 5.3.1.1)

 F5Y8D6_TREAZ            Unreviewed;       668 AA.
F5Y8D6;
27-JUL-2011, integrated into UniProtKB/TrEMBL.
27-JUL-2011, sequence version 1.
12-SEP-2018, entry version 59.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|HAMAP-Rule:MF_00147};
Includes:
RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147};
Short=TPI {ECO:0000256|HAMAP-Rule:MF_00147};
EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147};
AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
Includes:
RecName: Full=Phosphoglycerate kinase {ECO:0000256|HAMAP-Rule:MF_00145};
EC=2.7.2.3 {ECO:0000256|HAMAP-Rule:MF_00145};
Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145};
Synonyms=tpiA {ECO:0000256|HAMAP-Rule:MF_00147};
OrderedLocusNames=TREAZ_3384 {ECO:0000313|EMBL:AEF80328.1};
Treponema azotonutricium (strain ATCC BAA-888 / DSM 13862 / ZAS-9).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=545695 {ECO:0000313|EMBL:AEF80328.1, ECO:0000313|Proteomes:UP000009222};
[1] {ECO:0000313|Proteomes:UP000009222}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9
{ECO:0000313|Proteomes:UP000009222};
Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X.,
Lucey K., Ballor N.R., Ottesen E., Rosenthal R., Allen A.,
Leadbetter J.R., Paulsen I.T.;
"Complete sequence of Treponema azotonutricium strain ZAS-9.";
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
stereospecifically the conversion of dihydroxyacetone phosphate
(DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-
Rule:MF_00147}.
-!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
D-glyceroyl phosphate. {ECO:0000256|HAMAP-Rule:MF_00145,
ECO:0000256|SAAS:SAAS00676147}.
-!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
phosphate. {ECO:0000256|HAMAP-Rule:MF_00147,
ECO:0000256|SAAS:SAAS00958353}.
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
{ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|SAAS:SAAS00728615}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate from glycerone phosphate: step 1/1. {ECO:0000256|HAMAP-
Rule:MF_00147, ECO:0000256|SAAS:SAAS00728661}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
Rule:MF_00145, ECO:0000256|RuleBase:RU000695,
ECO:0000256|SAAS:SAAS00676133}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147,
ECO:0000256|SAAS:SAAS00728692}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145,
ECO:0000256|SAAS:SAAS00676135}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
ECO:0000256|RuleBase:RU000695, ECO:0000256|SAAS:SAAS00676138}.
-!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
{ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|SAAS:SAAS00676140}.
-!- SIMILARITY: Belongs to the triosephosphate isomerase family.
{ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|SAAS:SAAS00728708}.
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EMBL; CP001841; AEF80328.1; -; Genomic_DNA.
RefSeq; WP_015712185.1; NC_015577.1.
ProteinModelPortal; F5Y8D6; -.
STRING; 545695.TREAZ_3384; -.
EnsemblBacteria; AEF80328; AEF80328; TREAZ_3384.
KEGG; taz:TREAZ_3384; -.
eggNOG; ENOG4105BZA; Bacteria.
eggNOG; COG0126; LUCA.
eggNOG; COG0149; LUCA.
KO; K00927; -.
KO; K01803; -.
OMA; ERRHIFQ; -.
OrthoDB; POG091H00YN; -.
BioCyc; TAZO545695:G1GXX-2482-MONOMER; -.
UniPathway; UPA00109; UER00185.
UniPathway; UPA00109; UER00189.
UniPathway; UPA00138; -.
Proteomes; UP000009222; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-UniRule.
GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
CDD; cd00318; Phosphoglycerate_kinase; 1.
CDD; cd00311; TIM; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.40.50.1260; -; 3.
HAMAP; MF_00145; Phosphoglyc_kinase; 1.
HAMAP; MF_00147_B; TIM_B; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR001576; Phosphoglycerate_kinase.
InterPro; IPR015911; Phosphoglycerate_kinase_CS.
InterPro; IPR015824; Phosphoglycerate_kinase_N.
InterPro; IPR036043; Phosphoglycerate_kinase_sf.
InterPro; IPR035990; TIM_sf.
InterPro; IPR022896; TrioseP_Isoase_bac/euk.
InterPro; IPR000652; Triosephosphate_isomerase.
InterPro; IPR020861; Triosephosphate_isomerase_AS.
PANTHER; PTHR11406; PTHR11406; 2.
Pfam; PF00162; PGK; 1.
Pfam; PF00121; TIM; 1.
PRINTS; PR00477; PHGLYCKINASE.
SUPFAM; SSF51351; SSF51351; 1.
SUPFAM; SSF53748; SSF53748; 1.
TIGRFAMs; TIGR00419; tim; 1.
PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PROSITE; PS00171; TIM_1; 1.
PROSITE; PS51440; TIM_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00145,
ECO:0000256|SAAS:SAAS00676136};
Complete proteome {ECO:0000313|Proteomes:UP000009222};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
ECO:0000256|SAAS:SAAS00676144};
Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00147,
ECO:0000256|SAAS:SAAS00728593};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_00147,
ECO:0000256|RuleBase:RU000695, ECO:0000256|SAAS:SAAS00728672};
Isomerase {ECO:0000256|HAMAP-Rule:MF_00147,
ECO:0000256|SAAS:SAAS00498630, ECO:0000313|EMBL:AEF80328.1};
Kinase {ECO:0000256|HAMAP-Rule:MF_00145,
ECO:0000256|SAAS:SAAS00676134};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00145,
ECO:0000256|SAAS:SAAS00676136};
Reference proteome {ECO:0000313|Proteomes:UP000009222};
Transferase {ECO:0000256|HAMAP-Rule:MF_00145,
ECO:0000256|SAAS:SAAS00676134}.
NP_BIND 377 380 ATP. {ECO:0000256|HAMAP-Rule:MF_00145}.
REGION 20 22 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00145}.
REGION 59 62 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00145}.
REGION 428 430 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00147}.
REGION 652 653 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00147}.
ACT_SITE 513 513 Electrophile. {ECO:0000256|HAMAP-
Rule:MF_00147}.
ACT_SITE 585 585 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00147}.
BINDING 35 35 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00145}.
BINDING 138 138 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00145}.
BINDING 175 175 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00145}.
BINDING 226 226 ATP. {ECO:0000256|HAMAP-Rule:MF_00145}.
BINDING 317 317 ATP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00145}.
BINDING 348 348 ATP. {ECO:0000256|HAMAP-Rule:MF_00145}.
BINDING 591 591 Substrate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00147}.
BINDING 631 631 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00147}.
SEQUENCE 668 AA; 71166 MW; BE95B8C22621AB8C CRC64;
MIKTVKTVDL KGKRVIMRVD FNVPMKDGVV QDDTRITAAI PTIKYILGQG VKTLTLMSHL
GDPSKDAEKA KGKAEKDGKT FDLDKYIKGK HRMAPVAAYL SKKLKLPVVF AGEDSCYGKK
ALIDSQKPGT IIMLENTRFH KEETSKDDAQ RDKLAKALAE YGDIFVNDAF GTAHRDHAST
ASIAKFVPVS VAGFLMEKEV NYLEPIVTNP VKPLVAIIGG AKVSSKIAVL ESLLKNASAL
VIGGGMAYTF LKAQGKKIGK SLVEDDQIDT AKKILETAKK VGAEIVLPVD HVGADKFDAA
AEPVAVDNVN LPAKLMGLDV GPKTIAKYKE VLSKAKTIVW NGPVGVFEFD AFAKGTEAVA
KLVAEATARG AITVVGGGDS VAAVNKFGLA SKMSHVSTGG GASLELLEGK KLPGIEVTRS
RDYFIAGNWK MHKTRAEAAA LAKALVKALK PGKHKYLVAP TFTALETVGA IVKGTNILLG
AQNCAPEEQG AHTGEVSVLQ LKDLGVDAII LGHSERRHIY KEDDTLINKK VKLALKHGFE
VILCVGELLE EREKGKAEAV CKRQTEKGLA GVTPEELSKI TIAYEPVWAI GTGKTATPDD
AEAIHAYIRS VIAKLYGAQA AKQIVIQYGG SVKAENAAQL MAKEDIDGAL VGGAALKEET
FAPIAKFS


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