ID A0A1M5ZQS4_9VIBR Unreviewed; 762 AA.
AC A0A1M5ZQS4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN Name=ptsI_3 {ECO:0000313|EMBL:SHI26705.1};
GN ORFNames=VA7868_03091 {ECO:0000313|EMBL:SHI26705.1};
OS Vibrio aerogenes CECT 7868.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHI26705.1, ECO:0000313|Proteomes:UP000184608};
RN [1] {ECO:0000313|EMBL:SHI26705.1, ECO:0000313|Proteomes:UP000184608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7868 {ECO:0000313|EMBL:SHI26705.1,
RC ECO:0000313|Proteomes:UP000184608};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQXZ01000035; SHI26705.1; -; Genomic_DNA.
DR RefSeq; WP_073604710.1; NZ_FQXZ01000035.1.
DR AlphaFoldDB; A0A1M5ZQS4; -.
DR STRING; 1216006.VA7868_03091; -.
DR Proteomes; UP000184608; 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; IPR023151; PEP_util_CS.
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:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF01590; GAF; 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.
DR PROSITE; PS00742; PEP_ENZYMES_2; 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 Pyruvate {ECO:0000313|EMBL:SHI26705.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184608};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SHI26705.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..169
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 762 AA; 84261 MW; 98DF0F8099BA33B8 CRC64;
MRDMINADAL ASLTQIILSA AREDSVKEQV YHILEKLSET LQVDVCTLYR RQPDNSLKML
ATHGLIQTHP VILPEGEGLV GIILKNELPL NIIEPSQHPG YFYVRHSKEE KFRSFCGVPL
VYRGQVNGVL VVQSRQPVAL TPEQEAVLST IAIHLALLLD SFSSHEHLIT PENHLHRGVS
GAPGLTIGKV IIARHPELSA VTPIQIQDTM AELNRWQEIK NTALTEFARE KTLLQQAASK
GLASVTDVGK MMLQDPAFER IVTNEIAKGF HIPWGVKHAV SHFCEKFMAM HNPYLQARHE
DVEHLGDKLY QIWLGSDNLI ANDTGEPLIL IGERISVSTM AGLSTRNLTG IVCSCGASLS
HIAILANALG IPAVMGTGEL ALKDGDMIIV DGDRGEVIVS PGETLLAEYQ SLATERQQLS
DQLLALSDQP TRTKDNEPVL LLANTGLQAD IEPGLQYGAE GIGLFRTEIP FMASQALPSE
EDQVFLYNHV LSQYRDQPVC IRTLDVGSDK PLPYLPLIPE DNPALGLRGI RYTLDNLSLF
TTQLRALLRT TAEHPQLRLL LPMISTTEQL DMCLNLIDKL VDELREEGYQ VSRPPTGIMV
EVPGCIPLLP FWADKIDFIS VGTNDLSQYL LAVDRNNPLV SKWYHTLHPA ILHELMRIGR
LSKERDIPVS ICGEMAADPI AVVLLTGMGI RKLSMSASKI PLIKSLIREV SVQQCEALLD
QALALDTADK IYQLGNQFLM QHWSLAGNFT ERAPNPHEPI TI
//
