HUTX_VIBCH
ID HUTX_VIBCH Reviewed; 193 AA.
AC Q9KL40;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Intracellular heme transport protein HutX {ECO:0000303|PubMed:26807477};
DE AltName: Full=Heme-binding protein HutX {ECO:0000305};
GN Name=hutX {ECO:0000303|PubMed:25664785};
GN OrderedLocusNames=VC_A0908 {ECO:0000312|EMBL:AAF96805.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP CRYSTALLIZATION, HEME-BINDING, AND SUBUNIT.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=25664785; DOI=10.1107/s2053230x14027666;
RA Su T., Chi K., Wang K., Guo L., Huang Y.;
RT "Expression, purification and preliminary crystallographic analysis of a
RT haem-utilizing protein, HutX, from Vibrio cholerae.";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:141-144(2015).
RN [3] {ECO:0007744|PDB:5EXV}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 27-193, FUNCTION, HEME-BINDING,
RP SUBUNIT, INTERACTION WITH HUTZ, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 116-TYR-TYR-117.
RX PubMed=26807477; DOI=10.1021/acs.biochem.5b01273;
RA Sekine Y., Tanzawa T., Tanaka Y., Ishimori K., Uchida T.;
RT "Cytoplasmic heme-binding protein (HutX) from Vibrio cholerae is an
RT intracellular heme transport protein for the heme-degrading enzyme, HutZ.";
RL Biochemistry 55:884-893(2016).
CC -!- FUNCTION: Binds heme (PubMed:25664785, PubMed:26807477). Heme is
CC transferred to the heme-degrading enzyme HutZ via a specific protein-
CC protein interaction (PubMed:26807477). {ECO:0000269|PubMed:25664785,
CC ECO:0000269|PubMed:26807477}.
CC -!- SUBUNIT: Homodimer (PubMed:25664785, PubMed:26807477). Interacts with
CC HutZ (PubMed:26807477). {ECO:0000269|PubMed:25664785,
CC ECO:0000269|PubMed:26807477}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26807477}.
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DR EMBL; AE003853; AAF96805.1; -; Genomic_DNA.
DR PIR; B82403; B82403.
DR PDB; 5EXV; X-ray; 2.90 A; A/B/C/D/E/F=27-193.
DR PDBsum; 5EXV; -.
DR AlphaFoldDB; Q9KL40; -.
DR SMR; Q9KL40; -.
DR STRING; 243277.VC_A0908; -.
DR PRIDE; Q9KL40; -.
DR DNASU; 2612247; -.
DR EnsemblBacteria; AAF96805; AAF96805; VC_A0908.
DR KEGG; vch:VC_A0908; -.
DR eggNOG; COG3721; Bacteria.
DR HOGENOM; CLU_106714_0_0_6; -.
DR OMA; HSFGSIF; -.
DR BioCyc; VCHO:VCA0908-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16829; ChuX_HutX-like; 1.
DR InterPro; IPR010413; HutX-like.
DR Pfam; PF06228; ChuX_HutX; 1.
DR PIRSF; PIRSF030840; DUF1008; 1.
DR TIGRFAMs; TIGR04108; HutX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..193
FT /note="Intracellular heme transport protein HutX"
FT /id="PRO_0000446446"
FT BINDING 116
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:26807477"
FT MUTAGEN 116..117
FT /note="YY->FF: Weakens heme binding."
FT /evidence="ECO:0000269|PubMed:26807477"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:5EXV"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:5EXV"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:5EXV"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:5EXV"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5EXV"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:5EXV"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5EXV"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5EXV"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:5EXV"
SQ SEQUENCE 193 AA; 21714 MW; 328650E5DB40625D CRC64;
MYSGAYSFVQ ISTAAYRISI TRLEKTMESL QQQVAQLLEQ QPTLLPAAMA EQLNVTEFDI
VHALPEEMVA VVDGSHAQTI LESLPEWGPV TTIMTIAGSI FEVKAPFPKG KVARGYYNLM
GRDGELHGHL KLENISHVAL VSKPFMGRES HYFGFFTAQG ENAFKIYLGR DEKRELIPEQ
VARFKAMQQQ HKQ
