ID   BAHG_VITST              Reviewed;         146 AA.
AC   P04252;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Bacterial hemoglobin;
DE   AltName: Full=Soluble cytochrome O;
GN   Name=vhb;
OS   Vitreoscilla stercoraria.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Vitreoscilla.
OX   NCBI_TaxID=61;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3067078; DOI=10.1007/bf00340195;
RA   Khosla C., Bailey J.E.;
RT   "The Vitreoscilla hemoglobin gene: molecular cloning, nucleotide sequence
RT   and genetic expression in Escherichia coli.";
RL   Mol. Gen. Genet. 214:158-161(1988).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=3736670; DOI=10.1038/322481a0;
RA   Wakabayashi S., Matsubara H., Webster D.A.;
RT   "Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla.";
RL   Nature 322:481-483(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX   PubMed=2685332; DOI=10.1016/0022-2836(89)90292-1;
RA   Khosla C., Bailey J.E.;
RT   "Evidence for partial export of Vitreoscilla hemoglobin into the
RT   periplasmic space in Escherichia coli. Implications for protein function.";
RL   J. Mol. Biol. 210:79-89(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX   PubMed=2681149; DOI=10.1128/jb.171.11.5995-6004.1989;
RA   Khosla C., Bailey J.E.;
RT   "Characterization of the oxygen-dependent promoter of the Vitreoscilla
RT   hemoglobin gene in Escherichia coli.";
RL   J. Bacteriol. 171:5995-6004(1989).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).
RX   PubMed=9115439; DOI=10.1016/s0969-2126(97)00206-2;
RA   Tarricone C., Galizzi A., Coda A., Ascenzi P., Bolognesi M.;
RT   "Unusual structure of the oxygen-binding site in the dimeric bacterial
RT   hemoglobin from Vitreoscilla sp.";
RL   Structure 5:497-507(1997).
CC   -!- FUNCTION: This protein functions as a terminal oxidase.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; L21670; AAA75506.1; -; Genomic_DNA.
DR   EMBL; M30794; AAA27585.1; -; Genomic_DNA.
DR   EMBL; M27061; AAA27584.1; -; Genomic_DNA.
DR   PIR; S08307; GGZLB.
DR   PDB; 1VHB; X-ray; 1.83 A; A/B=1-146.
DR   PDB; 2VHB; X-ray; 1.76 A; A/B=1-146.
DR   PDB; 3TLD; X-ray; 1.90 A; A/B=1-146.
DR   PDB; 3TM3; X-ray; 1.75 A; A=1-146.
DR   PDB; 3TM9; X-ray; 1.72 A; A=1-146.
DR   PDB; 3VHB; X-ray; 2.10 A; A/B=1-146.
DR   PDB; 4VHB; X-ray; 1.80 A; A/B=1-146.
DR   PDBsum; 1VHB; -.
DR   PDBsum; 2VHB; -.
DR   PDBsum; 3TLD; -.
DR   PDBsum; 3TM3; -.
DR   PDBsum; 3TM9; -.
DR   PDBsum; 3VHB; -.
DR   PDBsum; 4VHB; -.
DR   AlphaFoldDB; P04252; -.
DR   SMR; P04252; -.
DR   DrugBank; DB03366; Imidazole.
DR   EvolutionaryTrace; P04252; -.
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:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0051409; P:response to nitrosative stress; IEA:InterPro.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR023950; Hmp.
DR   PANTHER; PTHR43396:SF3; PTHR43396:SF3; 1.
DR   Pfam; PF00042; Globin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..146
FT                   /note="Bacterial hemoglobin"
FT                   /id="PRO_0000052456"
FT   BINDING         53
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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:0000255|PROSITE-ProRule:PRU00238"
FT   HELIX           4..19
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           37..42
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           52..66
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           71..88
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           95..110
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:3TM9"
FT   HELIX           116..143
FT                   /evidence="ECO:0007829|PDB:3TM9"
SQ   SEQUENCE   146 AA;  15774 MW;  D8F96C641E7EF653 CRC64;
     MLDQQTINII KATVPVLKEH GVTITTTFYK NLFAKHPEVR PLFDMGRQES LEQPKALAMT
     VLAAAQNIEN LPAILPAVKK IAVKHCQAGV AAAHYPIVGQ ELLGAIKEVL GDAATDDILD
     AWGKAYGVIA DVFIQVEADL YAQAVE