ID A0A1I6SF39_9RHOB Unreviewed; 749 AA.
AC A0A1I6SF39;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=SAMN04488050_104328 {ECO:0000313|EMBL:SFS75582.1};
OS Alloyangia pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Alloyangia.
OX NCBI_TaxID=311180 {ECO:0000313|EMBL:SFS75582.1, ECO:0000313|Proteomes:UP000199392};
RN [1] {ECO:0000313|Proteomes:UP000199392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26894 {ECO:0000313|Proteomes:UP000199392};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; FOZW01000004; SFS75582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6SF39; -.
DR STRING; 311180.SAMN04488050_104328; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000199392; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFS75582.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..171
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 749 AA; 82701 MW; CB569140BEBB736D CRC64;
MPDGTESESR KLLGRLRDTM AEDAAGQARL DKITHLTADS MGSEVCSIYL FRDEDTLELC
ATEGLKKEAV HQTRMRMGEG LVGRVARSGK VVNTADAPSA KGFRYMPETG EEIYSSFLGV
PIQRLGETLG VLVVQTKQKR EFTSDEVYAL EVVAMVLAEM TELGAFVGDT AALSARHTQP
TMLRGGTGQE GTTEGHVWLH EPRVMVTNLV ADDPERELQR LDAAIEQLRV SVDEMLAGAV
EDAEQLEVLE AYRMFANSKG WRRRMEEDIS RGLSAEAAVE KEQSAARARM SQVADNYLRE
RLHDLDDLSN RLLRILTGQG KDTGASMPAD PILVARNIGP GELLEYGRQL RGIVLEEGSV
GSHAAVVARA LAIPLVINAT RITTEALNGD HIMVDGDQGL VHLRPDDTVV TAFRDKIAMQ
AEAQERYASI RQKPAISQCG KRISLYMNAG LLADLPSLEN SGAEGVGLFR TELQFLVRNK
MPSRTELVAV YKRVIEAAEA AGDKPVIFRT LDIGSDKVLP YMKPTDEPNP ALGWRAIRVG
LDRPGVMRMQ LQALLRASEG RPLTLMFPFV AQWEEFRAAR AEVDKAMAIE RKLGHVVPEK
ISVGTMLETP SLAYASNKFF EEVEFVSIGG NDLKQFFFAA DRENERVRRR YDTLNVSFLT
FLEQIVQRCS ATGTPLSFCG EDAGRPIEAI CLAAIGLHRL SMRPASIGPV KSLIMRTDLD
ALYDVICDAR ERGEQSVRGA VMDFMRWQG
//