HBB_LEIXA
ID HBB_LEIXA Reviewed; 147 AA.
AC P56251;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=hbb;
OS Leiostomus xanthurus (Spot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Leiostomus.
OX NCBI_TaxID=59837;
RN [1]
RP PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX
RP WITH HEME.
RX PubMed=8605630; DOI=10.1038/nsb0396-275;
RA Mylvaganam S.E., Bonaventura C., Bonaventura J., Getzoff E.D.;
RT "Structural basis for the root effect in haemoglobin.";
RL Nat. Struct. Biol. 3:275-283(1996).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PDB; 1SPG; X-ray; 1.95 A; B=1-147.
DR PDBsum; 1SPG; -.
DR AlphaFoldDB; P56251; -.
DR SMR; P56251; -.
DR MINT; P56251; -.
DR EvolutionaryTrace; P56251; -.
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:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR CDD; cd08925; Hb-beta-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; IPR002337; Hemoglobin_b.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00814; BETAHAEM.
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..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052988"
FT BINDING 63
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:0000250|UniProtKB:P80044"
FT BINDING 92
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:0000269|PubMed:8605630,
FT ECO:0007744|PDB:1SPG"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:1SPG"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:1SPG"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:1SPG"
SQ SEQUENCE 147 AA; 16294 MW; 253C91230838BE0C CRC64;
VDWTDAERAA IKALWGKIDV GEIGPQALSR LLIVYPWTQR HFKGFGNIST NAAILGNAKV
AEHGKTVMGG LDRAVQNMDN IKNVYKQLSI KHSEKIHVDP DNFRLLGEII TMCVGAKFGP
SAFTPEIHEA WQKFLAVVVS ALGRQYH
