ID A0A238D5W5_THIDL Unreviewed; 151 AA.
AC A0A238D5W5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Group 1 truncated hemoglobin {ECO:0000256|PIRNR:PIRNR002030};
GN ORFNames=THIARS_70338 {ECO:0000313|EMBL:SBP88718.1};
OS Thiomonas delicata (Thiomonas cuprina).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=364030 {ECO:0000313|EMBL:SBP88718.1, ECO:0000313|Proteomes:UP000214566};
RN [1] {ECO:0000313|EMBL:SBP88718.1, ECO:0000313|Proteomes:UP000214566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16361 {ECO:0000313|EMBL:SBP88718.1,
RC ECO:0000313|Proteomes:UP000214566};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR002030-1};
CC Note=Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR002030-1};
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group I
CC subfamily. {ECO:0000256|ARBA:ARBA00009660,
CC ECO:0000256|PIRNR:PIRNR002030}.
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DR EMBL; FLMQ01000056; SBP88718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238D5W5; -.
DR OrthoDB; 9795814at2; -.
DR Proteomes; UP000214566; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR CDD; cd00454; TrHb1_N; 1.
DR Gene3D; 1.10.490.10; Globins; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR InterPro; IPR016339; Hemoglobin_trunc_I.
DR Pfam; PF01152; Bac_globin; 1.
DR PIRSF; PIRSF002030; Globin_Protozoa/Cyanobacteria; 1.
DR SUPFAM; SSF46458; Globin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|PIRNR:PIRNR002030, ECO:0000256|PIRSR:PIRSR002030-1};
KW Iron {ECO:0000256|PIRNR:PIRNR002030, ECO:0000256|PIRSR:PIRSR002030-1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR002030,
KW ECO:0000256|PIRSR:PIRSR002030-1};
KW Oxygen transport {ECO:0000256|PIRNR:PIRNR002030};
KW Reference proteome {ECO:0000313|Proteomes:UP000214566};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|PIRNR:PIRNR002030}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..151
FT /note="Group 1 truncated hemoglobin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013099399"
FT BINDING 103
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR601486-1"
FT BINDING 103
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR002030-1"
SQ SEQUENCE 151 AA; 16623 MW; 756DF2A5CCE2A799 CRC64;
MKLQSPHLTR HLAGVVLTCA MALPTFAHAE MASGPTLYEQ LGGKPAIVMI VHDMLANVVA
DNRINHYFAK TNIPHLQMEL VSQICELTDG PCKYTGLNMQ QAHRGMNLKT ADFNALVEDL
QKSMNSNNVP LGLQNQLLNI LAPMEPDVVH K
//