ID   GLBB_RIFPA              Reviewed;         144 AA.
AC   P80592;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Giant hemoglobins B chain;
OS   Riftia pachyptila (Vent tube worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Canalipalpata; Sabellida; Siboglinidae; Riftia.
OX   NCBI_TaxID=6426;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=9408952;
RX   DOI=10.1002/(sici)1097-0134(199712)29:4<562::aid-prot15>3.0.co;2-k;
RA   Zal F., Suzuki T., Kawasaki Y., Childress J.J., Lallier F.H., Toulmond A.;
RT   "Primary structure of the common polypeptide chain b from the multi-
RT   hemoglobin system of the hydrothermal vent tube worm Riftia pachyptila: an
RT   insight on the sulfide binding-site.";
RL   Proteins 29:562-574(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=15710902; DOI=10.1073/pnas.0407455102;
RA   Flores J.F., Fisher C.R., Carney S.L., Green B.N., Freytag J.K.,
RA   Schaeffer S.W., Royer W.E. Jr.;
RT   "Sulfide binding is mediated by zinc ions discovered in the crystal
RT   structure of a hydrothermal vent tubeworm hemoglobin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:2713-2718(2005).
CC   -!- SUBUNIT: Part of giant hemoglobin C1, V1 and V2. This worm has three
CC       different extracellular Hbs: two dissolved in the vascular blood, V1
CC       (CA. 3,500 kDa) and V2 (CA. 400 kDa), and one in the coelomic fluid, C1
CC       (CA. 400 kDa). V1 consists of four heme-containing, globin chains (B-E)
CC       and four linker chains (L1-L4). V2 consists of six globin chains (A-F)
CC       and C1 consists of five globin chains (A-E).
CC       {ECO:0000269|PubMed:15710902}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PDB; 1YHU; X-ray; 3.15 A; B/F/J/N/R/V=1-144.
DR   PDBsum; 1YHU; -.
DR   AlphaFoldDB; P80592; -.
DR   SMR; P80592; -.
DR   EvolutionaryTrace; P80592; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd01040; Mb-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR014610; Haemoglobin_extracell.
DR   InterPro; IPR044399; Mb-like_M.
DR   Pfam; PF00042; Globin; 1.
DR   PIRSF; PIRSF036517; Ext_hemo; 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; Secreted; Transport.
FT   CHAIN           1..144
FT                   /note="Giant hemoglobins B chain"
FT                   /id="PRO_0000052509"
FT   BINDING         96
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   HELIX           6..19
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   HELIX           26..40
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   TURN            52..54
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   HELIX           59..78
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   HELIX           82..96
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   HELIX           103..121
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:1YHU"
FT   HELIX           128..143
FT                   /evidence="ECO:0007829|PDB:1YHU"
SQ   SEQUENCE   144 AA;  16135 MW;  9A094A9E8E981568 CRC64;
     DYVCGPLQRL KVKRQWAEAY GSGNSREEFG HFIWSHVFQH SPAARDMFKR VRGDNIHTPA
     FRAHATRVLG GLDMCIALLD DEPVLNTQLA HLAKQHETRG VEAAHYDTVN HAVMMGVENV
     IGSEVFDQDA WKPCLNVITN GIQG