ID A0A0C2G0E1_9ACTN Unreviewed; 135 AA.
AC A0A0C2G0E1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Group 1 truncated hemoglobin {ECO:0000256|PIRNR:PIRNR002030};
GN ORFNames=LP52_22885 {ECO:0000313|EMBL:KIH96783.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH96783.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIH96783.1}.
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DR EMBL; JROO01000048; KIH96783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2G0E1; -.
DR STRING; 183763.LP52_22885; -.
DR Proteomes; UP000031675; 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 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 Receptor {ECO:0000313|EMBL:KIH96783.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031675};
KW Transport {ECO:0000256|PIRNR:PIRNR002030}.
FT BINDING 77
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 77
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"
FT BINDING 120
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"
SQ SEQUENCE 135 AA; 14154 MW; D94FA6810F1C5EFD CRC64;
MPIVTNDSVS IYERIGGHEA IAAVVDDLYV RIMDDPQLEG FFTGSNLAKL KGRQVEFFSA
ALGGPNVYDG GAMDEVHRGR GIEQHHFDLV ADHLVASLKG AGVPADTVDE IIGVVAPLSH
DIVGGSSKTP SAAAD
//
