HMP_VIBCH
ID HMP_VIBCH Reviewed; 394 AA.
AC Q9KMY3;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Flavohemoprotein;
DE AltName: Full=Flavohemoglobin;
DE AltName: Full=Hemoglobin-like protein;
DE AltName: Full=Nitric oxide dioxygenase;
DE Short=NO oxygenase;
DE Short=NOD;
DE EC=1.14.12.17;
GN Name=hmp; OrderedLocusNames=VC_A0183;
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).
CC -!- FUNCTION: Is involved in NO detoxification in an aerobic process,
CC termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and
CC NAD(P)H to convert NO to nitrate, which protects the bacterium from
CC various noxious nitrogen compounds. Therefore, plays a central role in
CC the inducible response to nitrosative stress (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate;
CC Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.12.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate;
CC Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.12.17;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- DOMAIN: Consists of two distinct domains; an N-terminal heme-containing
CC oxygen-binding domain and a C-terminal reductase domain with binding
CC sites for FAD and NAD(P)H.
CC -!- SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000305}.
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DR EMBL; AE003853; AAF96096.1; -; Genomic_DNA.
DR PIR; F82491; F82491.
DR RefSeq; NP_232583.1; NC_002506.1.
DR RefSeq; WP_000957478.1; NZ_LT906615.1.
DR PDB; 4EH1; X-ray; 2.20 A; A/B=152-394.
DR PDBsum; 4EH1; -.
DR AlphaFoldDB; Q9KMY3; -.
DR SMR; Q9KMY3; -.
DR STRING; 243277.VC_A0183; -.
DR DNASU; 2611856; -.
DR EnsemblBacteria; AAF96096; AAF96096; VC_A0183.
DR GeneID; 57741636; -.
DR KEGG; vch:VC_A0183; -.
DR PATRIC; fig|243277.26.peg.2821; -.
DR eggNOG; COG1017; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_12_0_6; -.
DR OMA; ADIHYEV; -.
DR BioCyc; VCHO:VCA0183-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008941; F:nitric oxide dioxygenase activity; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IBA:GO_Central.
DR GO; GO:0046210; P:nitric oxide catabolic process; IBA:GO_Central.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_01252; Hmp; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR023950; Hmp.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43396:SF3; PTHR43396:SF3; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF46458; SSF46458; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW NAD; NADP; Oxidoreductase; Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..394
FT /note="Flavohemoprotein"
FT /id="PRO_0000052449"
FT DOMAIN 152..262
FT /note="FAD-binding FR-type"
FT REGION 1..140
FT /note="Globin"
FT REGION 149..394
FT /note="Reductase"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 206..209
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 274..279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 385..388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT SITE 29
FT /note="Involved in heme-bound ligand stabilization and O-O
FT bond activation"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000250"
FT SITE 384
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000250"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 166..178
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:4EH1"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:4EH1"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:4EH1"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4EH1"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:4EH1"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4EH1"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:4EH1"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:4EH1"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:4EH1"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:4EH1"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:4EH1"
SQ SEQUENCE 394 AA; 44191 MW; DDA3490FAE28823A CRC64;
MLTQEHINII KSTIPLLESA GPALTQHFYQ RMFSHNPELK HIFNMTHQKT GRQSVALFEA
IAAYAKHIDN LAALTSAVER IAHKHTSFNI QPEHYQIVGH HLLETLRELA PDAFTQPVEE
AWTAAYFFLA QVFIDREGAL YLERKQALGG WRDGRTFVVR EKQVESAYVT SFVLVPADGG
AVLDYQPGQY IGIEVTPEGS DYREIRQYSL SHASNGREYR ISVKREGVGS DNPGLVSHYL
HNNVKVGDSV KLYAPAGDFF YVERERPVVL ISAGVGATPM QAILHTLAKQ NKSGVTYLYA
CNSAKEHTFA QETAQLIAQQ GWMQQVWYRD ESADDVLQGE MQLAELILPI EDGDFYLCGP
IGFMQYVVKQ LLALGVDKAR IHYEVFGPHA QLAA
