HBB_ALDGI
ID HBB_ALDGI Reviewed; 146 AA.
AC P83133;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Hemoglobin A/D subunit beta;
DE AltName: Full=Hemoglobin A/D beta chain;
OS Aldabrachelys gigantea (Aldabra giant tortoise) (Geochelone gigantea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Aldabrachelys.
OX NCBI_TaxID=167804 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Erythrocyte;
RA Shishikura F., Takami K.;
RT "The amino acid sequences of the alpha- and beta-globin chains of
RT hemoglobin from the Aldabra giant tortoises, Geochelone gigantea.";
RL Zool. Sci. 18:515-526(2001).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000250|UniProtKB:P13274}.
CC -!- SUBUNIT: Hemoglobins A and D are heterotetramers of alpha-1, alpha-2
CC and two identical beta chains. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MISCELLANEOUS: Hemoglobin A is the major, and hemoglobin D the minor
CC hemoglobin of this species. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PDB; 1V75; X-ray; 2.02 A; B=1-146.
DR PDB; 1WMU; X-ray; 1.65 A; B=1-146.
DR PDB; 2Z6N; X-ray; 1.86 A; B=1-146.
DR PDBsum; 1V75; -.
DR PDBsum; 1WMU; -.
DR PDBsum; 2Z6N; -.
DR AlphaFoldDB; P83133; -.
DR SMR; P83133; -.
DR EvolutionaryTrace; P83133; -.
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..146
FT /note="Hemoglobin A/D subunit beta"
FT /id="PRO_0000052861"
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:0000255|PROSITE-ProRule:PRU00238"
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:0000255|PROSITE-ProRule:PRU00238"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:1WMU"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1WMU"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:1WMU"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1WMU"
SQ SEQUENCE 146 AA; 16174 MW; A66CB0866946902F CRC64;
VHWTSEEKQY ITSLWAKVNV GEVGGEALAR LLIVYPWTQR FFASFGNLSS ANAILHNAKV
LAHGQKVLTS FGEAVKNLDN IKKTFAQLSE LHCEKLHVDP ENFKLLGNIL IIVLATHFPK
EFTPASQAAW TKLVNAVAHA LALGYH
