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Database: UniProt
Entry: A0A1I6SF39_9RHOB
LinkDB: A0A1I6SF39_9RHOB
Original site: A0A1I6SF39_9RHOB 
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
//
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