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Database: UniProt
Entry: A0A0J1GHM1_9GAMM
LinkDB: A0A0J1GHM1_9GAMM
Original site: A0A0J1GHM1_9GAMM 
ID   A0A0J1GHM1_9GAMM        Unreviewed;       829 AA.
AC   A0A0J1GHM1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=PTS fructose transporter subunit IIA {ECO:0000313|EMBL:KLU99179.1};
GN   ORFNames=ABT58_19430 {ECO:0000313|EMBL:KLU99179.1};
OS   Photobacterium aphoticum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU99179.1, ECO:0000313|Proteomes:UP000036426};
RN   [1] {ECO:0000313|EMBL:KLU99179.1, ECO:0000313|Proteomes:UP000036426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU99179.1,
RC   ECO:0000313|Proteomes:UP000036426};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         fructose 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC         ChEBI:CHEBI:64837; EC=2.7.1.202;
CC         Evidence={ECO:0000256|ARBA:ARBA00001401};
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}.
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:KLU99179.1}.
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DR   EMBL; LDOV01000037; KLU99179.1; -; Genomic_DNA.
DR   RefSeq; WP_047876098.1; NZ_PYMF01000005.1.
DR   AlphaFoldDB; A0A0J1GHM1; -.
DR   PATRIC; fig|754436.4.peg.4112; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000036426; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   Gene3D; 3.30.1340.10; HPr-like; 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; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_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; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR006318; PTS_EI-like.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR008731; PTS_EIN.
DR   InterPro; IPR001020; PTS_HPr_His_P_site.
DR   InterPro; IPR004715; PTS_IIA_fruc.
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; TIGR00848; fruA; 1.
DR   NCBIfam; TIGR01417; PTS_I_fam; 1.
DR   PANTHER; PTHR46244:SF4; MULTIPHOSPHORYL TRANSFER PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   PRINTS; PR01736; PHPHTRNFRASE.
DR   SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR   SUPFAM; SSF55594; HPr-like; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
DR   PROSITE; PS00369; PTS_HPR_HIS; 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   Reference proteome {ECO:0000313|Proteomes:UP000036426};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          2..94
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
FT   DOMAIN          683..826
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   829 AA;  90852 MW;  8C87DA5676F563B1 CRC64;
     MKHELSFRCT LPNGIHARPA SHLEKACQPF QCQITLINHR NGNRGNAKSV LAIVGTDTLL
     NDDCTLLFEG ADSTEALATL TPYMTEVFPY CDEALAITGE ADTVVMPQSL MRLQPNLIHG
     TRLAQGIAHG TLVSFQHIDL MQFATPSQGD EYDRFSDAHQ QVTANLNQAI AQASAHEKAI
     LDAHLAILQD ATFVNGITAL LPTHSTADAI LAMVEQLSAQ LQQSSSAYLR ERVLDIRDIA
     TQLLLAAYPH VECQRDFVLT APSIVIANDL TPSQFLALDK NRLQGLILTQ AGSTSHTVIL
     ARAFNIPTLS GIELNECVPA LNTPVYLDAQ LGVVALHANT AVQRYFNRAL ALQASQQQRQ
     HSFAMQAAHT LDGHHIEVAA NIACTIEADA AFQQGAEGIG LFRTEMLFMD RPQAPNEEEQ
     VQHYRDVLTA ANGKPVIIRT MDIGGDKPID YLDLPAENNP FLGYRAVRIY PQFLPLFHTQ
     LRAILRASAY GNAKVMIPMI QSIEEIRWVK AQLDIVKVQL DNAGIAYDTN LQLGIMVEVP
     SVAFIIDQFC QEVDFFSIGS NDMTQYLLAV DRDNANVAPL YNSLSPAFLR MLGLIVETAH
     QHGRWVGLCG ELGADTRVLP LLVGAGLDEI SMSAPKIAAA KTALREWRLE HCQNLFANAC
     QCSTIADVNA LLDNAQREQA NKPLLGVECM FTQADFASKE EAIQALVGNL GVTGRTNDIY
     KLEEDIWARE AVFSTGLGHG FAIPHTKSAN ILHSSISIAK LNAPIDWQSD SGEADFIIML
     TLNHEQGDQH MRIFSSLARK LIHPSFRDSL KACESGEAMI ALLQQELAL
//
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