GLB1_PHAPT
ID GLB1_PHAPT Reviewed; 143 AA.
AC P41260; Q9GV87;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Hemoglobin-1;
DE AltName: Full=Hemoglobin I;
DE Short=Hb I;
DE Short=HbI;
DE AltName: Full=Sulfide-reactive hemoglobin;
OS Phacoides pectinatus (Thick lucine) (Lucina pectinata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Lucinida;
OC Lucinoidea; Lucinidae; Phacoides.
OX NCBI_TaxID=244486;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10839619; DOI=10.1023/a:1020623011363;
RA Antommattei-Perez F.M., Rosado-Ruiz T., Cadilla C.L., Lopez-Garriga J.;
RT "The cDNA-derived amino acid sequence of hemoglobin I from Lucina
RT pectinata.";
RL J. Protein Chem. 18:831-836(1999).
RN [2]
RP CHARACTERIZATION.
RX PubMed=2398044; DOI=10.1016/s0021-9258(17)46185-0;
RA Kraus D.W., Wittenberg J.B.;
RT "Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular
RT properties, kinetics and equilibria of reactions with ligands.";
RL J. Biol. Chem. 265:16043-16053(1990).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2, AND X-RAY CRYSTALLOGRAPHY
RP (1.5 ANGSTROMS).
RC TISSUE=Gill;
RX PubMed=7966324; DOI=10.1006/jmbi.1994.1706;
RA Rizzi M., Wittenberg J.B., Coda A., Ascenzi P., Fasano M., Bolognesi M.;
RT "Structure of the sulfide-reactive hemoglobin from the clam Lucina
RT pectinata. Crystallographic analysis at 1.5-A resolution.";
RL J. Mol. Biol. 244:86-99(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8613980; DOI=10.1006/jmbi.1996.0228;
RA Rizzi M., Wittenberg J.B., Coda A., Ascenzi P., Bolognesi M.;
RT "Structural bases for sulfide recognition in Lucina pectinata hemoglobin
RT I.";
RL J. Mol. Biol. 258:1-5(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=10423453; DOI=10.1016/s0006-3495(99)76959-6;
RA Bolognesi M., Rosano C., Losso R., Borassi A., Rizzi M., Wittenberg J.B.,
RA Boffi A., Ascenzi P.;
RT "Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale
RT myoglobin: an X-ray crystallographic study.";
RL Biophys. J. 77:1093-1099(1999).
CC -!- FUNCTION: Serves to transport hydrogen sulfide to autotrophic bacteria.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: This molluscan globin lacks one of the heme-binding
CC histidine residues found in most other globins.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AF187049; AAG01380.1; -; mRNA.
DR PDB; 1B0B; X-ray; 1.43 A; A=2-141.
DR PDB; 1EBT; X-ray; 1.90 A; A=2-143.
DR PDB; 1FLP; X-ray; 1.50 A; A=2-143.
DR PDB; 1MOH; X-ray; 1.90 A; A=2-143.
DR PDBsum; 1B0B; -.
DR PDBsum; 1EBT; -.
DR PDBsum; 1FLP; -.
DR PDBsum; 1MOH; -.
DR AlphaFoldDB; P41260; -.
DR SMR; P41260; -.
DR iPTMnet; P41260; -.
DR EvolutionaryTrace; P41260; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005833; C:hemoglobin complex; 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:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0015671; P:oxygen transport; IEA:InterPro.
DR CDD; cd01040; Mb-like; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR002336; Erythrocruorin.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR044399; Mb-like_M.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00611; ERYTHCRUORIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Heme;
KW Iron; Metal-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..143
FT /note="Hemoglobin-1"
FT /id="PRO_0000052492"
FT BINDING 97
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:7966324"
FT CONFLICT 49
FT /note="K -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..36
FT /evidence="ECO:0007829|PDB:1B0B"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1B0B"
FT TURN 43..50
FT /evidence="ECO:0007829|PDB:1B0B"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1B0B"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:1B0B"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:1B0B"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:1B0B"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:1B0B"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1B0B"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:1B0B"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1B0B"
SQ SEQUENCE 143 AA; 14944 MW; 0DFB3A709E97BED5 CRC64;
MSLSAAQKDN VKSSWAKASA AWGTAGPEFF MALFDAHDDV FAKFSGLFKG AAKGTVKNTP
EMAAQAQSFK GLVSNWVDNL DNAGALEGQC KTFAANHKAR GISAGQLEAA FKVLAGFMKS
YGGDEGAWTA VAGALMGMIR PNM
