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Database: UniProt
Entry: M7NIH3_9BACL
LinkDB: M7NIH3_9BACL
Original site: M7NIH3_9BACL 
ID   M7NIH3_9BACL            Unreviewed;       394 AA.
AC   M7NIH3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Flavohemoprotein {ECO:0000256|HAMAP-Rule:MF_01252};
DE   AltName: Full=Flavohemoglobin {ECO:0000256|HAMAP-Rule:MF_01252};
DE   AltName: Full=Hemoglobin-like protein {ECO:0000256|HAMAP-Rule:MF_01252};
DE   AltName: Full=Nitric oxide dioxygenase {ECO:0000256|HAMAP-Rule:MF_01252};
DE            Short=NO oxygenase {ECO:0000256|HAMAP-Rule:MF_01252};
DE            Short=NOD {ECO:0000256|HAMAP-Rule:MF_01252};
DE            EC=1.14.12.17 {ECO:0000256|HAMAP-Rule:MF_01252};
GN   Name=hmp {ECO:0000256|HAMAP-Rule:MF_01252,
GN   ECO:0000313|EMBL:EMR07052.1};
GN   ORFNames=C772_00697 {ECO:0000313|EMBL:EMR07052.1};
OS   Bhargavaea cecembensis DSE10.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX   NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR07052.1, ECO:0000313|Proteomes:UP000011919};
RN   [1] {ECO:0000313|EMBL:EMR07052.1, ECO:0000313|Proteomes:UP000011919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE10 {ECO:0000313|EMBL:EMR07052.1,
RC   ECO:0000313|Proteomes:UP000011919};
RX   PubMed=23766406;
RA   Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT   from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT   Chagos-Laccadive Ridge System in the Indian Ocean.";
RL   Genome Announc. 1:e00346-13(2013).
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01252}.
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         Evidence={ECO:0000256|ARBA:ARBA00000126, ECO:0000256|HAMAP-
CC         Rule:MF_01252};
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         Evidence={ECO:0000256|ARBA:ARBA00001762, ECO:0000256|HAMAP-
CC         Rule:MF_01252};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01252};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01252};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01252};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01252};
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. {ECO:0000256|HAMAP-Rule:MF_01252}.
CC   -!- SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins
CC       subfamily. {ECO:0000256|ARBA:ARBA00008414, ECO:0000256|HAMAP-
CC       Rule:MF_01252}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC       {ECO:0000256|ARBA:ARBA00006401, ECO:0000256|HAMAP-Rule:MF_01252}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00238}.
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:EMR07052.1}.
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DR   EMBL; AOFT01000003; EMR07052.1; -; Genomic_DNA.
DR   RefSeq; WP_008297461.1; NZ_AOFT01000003.1.
DR   AlphaFoldDB; M7NIH3; -.
DR   STRING; 1235279.C772_00697; -.
DR   PATRIC; fig|1235279.3.peg.713; -.
DR   eggNOG; COG1017; Bacteria.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000011919; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051409; P:response to nitrosative stress; IEA:InterPro.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR   CDD; cd14777; Yhb1-globin-like; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_01252; Hmp; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
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; FLAVOHEMOPROTEIN; 1.
DR   PANTHER; PTHR43396:SF3; FLAVOHEMOPROTEIN; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00042; Globin; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   3: Inferred from homology;
KW   Detoxification {ECO:0000256|HAMAP-Rule:MF_01252};
KW   Dioxygenase {ECO:0000313|EMBL:EMR07052.1};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_01252};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01252};
KW   Heme {ECO:0000256|HAMAP-Rule:MF_01252, ECO:0000256|RuleBase:RU000356};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01252};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01252};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01252};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01252};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01252,
KW   ECO:0000313|EMBL:EMR07052.1};
KW   Oxygen transport {ECO:0000256|ARBA:ARBA00022621, ECO:0000256|HAMAP-
KW   Rule:MF_01252}; Reference proteome {ECO:0000313|Proteomes:UP000011919};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01252, ECO:0000256|RuleBase:RU000356}.
FT   DOMAIN          1..134
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          152..261
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          149..394
FT                   /note="Reductase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT   ACT_SITE        95
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT   ACT_SITE        137
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
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:0000256|HAMAP-Rule:MF_01252"
FT   BINDING         190
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT   BINDING         206..209
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT   BINDING         274..279
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT   BINDING         382..385
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT   SITE            29
FT                   /note="Involved in heme-bound ligand stabilization and O-O
FT                   bond activation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT   SITE            84
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
FT   SITE            381
FT                   /note="Influences the redox potential of the prosthetic
FT                   heme and FAD groups"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01252"
SQ   SEQUENCE   394 AA;  43364 MW;  689F96408FE51A61 CRC64;
     MLSQQTIDIV KSTVPVLEQH GKTITTVFYK NMFEAHPELL NIFNHANQSR GRQQTALANT
     VLAAAKYIDN LEAIVPAVVQ IAHKHRGLDV RPEHYPIVGH HLLGAIKEVL GDAATPEILN
     AWGEAYGVIA DAFIGVEKSM YDEAANSENG WDGFKDFVVA KKVEESDVIT SFYLKPADGK
     GVPTYKPGQY LTIRVTIPGE KYMMIRQYSL SRAPQEDMFR ISVKREDECN PEGKVSTFLH
     RSVNVGDRIE VSAPAGDFFL HTEATTPVTL ISGGVGLTPM MAMFDHITSN QPERKAAFIH
     SARNPQLQAF DGDLREMAAG NDNATYSVRY SDTEGFLDRG FLSSRVIEGS DVYLCGPAAF
     MNAMIHELKA IGVPVGKIHY EFFGPAAELE AITA
//
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