TRHBO_MYCLE
ID TRHBO_MYCLE Reviewed; 128 AA.
AC Q9CC59;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Group 2 truncated hemoglobin GlbO;
DE AltName: Full=Hemoglobin-like protein HbO;
DE AltName: Full=Truncated hemoglobin;
DE Short=TrHbO;
GN Name=glbO; OrderedLocusNames=ML1253;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC -!- PTM: Contains L-DOPA (3',4'-dihydroxyphenylalanine).
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group II
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL583921; CAC31634.1; -; Genomic_DNA.
DR PIR; G87065; G87065.
DR RefSeq; NP_301903.1; NC_002677.1.
DR RefSeq; WP_010908224.1; NC_002677.1.
DR AlphaFoldDB; Q9CC59; -.
DR SMR; Q9CC59; -.
DR STRING; 272631.ML1253; -.
DR EnsemblBacteria; CAC31634; CAC31634; CAC31634.
DR KEGG; mle:ML1253; -.
DR PATRIC; fig|272631.5.peg.2309; -.
DR Leproma; ML1253; -.
DR eggNOG; COG2346; Bacteria.
DR HOGENOM; CLU_103526_3_1_11; -.
DR OMA; QYWGGPT; -.
DR Proteomes; UP000000806; Chromosome.
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 Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR019795; Globin_bac-like_CS.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR Pfam; PF01152; Bac_globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01213; GLOBIN_FAM_2; 1.
PE 3: Inferred from homology;
KW Heme; Hydroxylation; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT CHAIN 1..128
FT /note="Group 2 truncated hemoglobin GlbO"
FT /id="PRO_0000162642"
FT BINDING 75
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:0000250"
FT MOD_RES 36
FT /note="3',4'-dihydroxyphenylalanine"
FT /evidence="ECO:0000250"
FT CROSSLNK 23..36
FT /note="Isodityrosine (Tyr-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 128 AA; 14829 MW; D33EBC2984DD3853 CRC64;
MQQSFYDAIG GAETFKAIVS RFYAQVPEDE ILRELYPADD LAGAEERLRM FLEQYWGGPR
TYSSQRGHPR LRMRHAPFRI TAIERDAWLR CMHTAVASID SHTLDNEHRR ELLDYLEMAA
HSLVNSAS