ID A0A0Q8NS87_9ACTN Unreviewed; 253 AA.
AC A0A0Q8NS87;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Antibiotic biosynthesis monooxygenase {ECO:0000313|EMBL:KRB64037.1};
GN ORFNames=ASE03_05705 {ECO:0000313|EMBL:KRB64037.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB64037.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB64037.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB64037.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB64037.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB64037.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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:KRB64037.1}.
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DR EMBL; LMHX01000034; KRB64037.1; -; Genomic_DNA.
DR RefSeq; WP_057234133.1; NZ_LMHX01000034.1.
DR AlphaFoldDB; A0A0Q8NS87; -.
DR STRING; 1736486.ASE03_05705; -.
DR Proteomes; UP000051829; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; 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; cd14775; TrHb2_O-like; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 1.10.490.10; Globins; 1.
DR InterPro; IPR007138; ABM_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR Pfam; PF03992; ABM; 1.
DR Pfam; PF01152; Bac_globin; 1.
DR SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR SUPFAM; SSF46458; Globin-like; 1.
DR PROSITE; PS51725; ABM; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR601486-1};
KW Iron {ECO:0000256|PIRSR:PIRSR601486-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601486-1};
KW Monooxygenase {ECO:0000313|EMBL:KRB64037.1};
KW Oxidoreductase {ECO:0000313|EMBL:KRB64037.1};
KW Oxygen transport {ECO:0000256|ARBA:ARBA00022621};
KW Reference proteome {ECO:0000313|Proteomes:UP000051829};
KW Transport {ECO:0000256|ARBA:ARBA00022621}.
FT DOMAIN 2..92
FT /note="ABM"
FT /evidence="ECO:0000259|PROSITE:PS51725"
FT BINDING 148
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 172
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 253 AA; 28622 MW; 6F924D0B40EA9CB7 CRC64;
MIVEYIRYRI AEPQRAAFEQ AYLRAADPLG AAEQCVDYEL ARCTEEPAAY VLRIRWTSAE
DHLGGFRKGE HFAAFFAEIK PYVESIEEMR HYEVTSVEGK GGSTPTLYEW AGGADAFDRL
FTRFYERVPE DEILAPVFAG MDPQHAQHVA AWLGEVFGGP ARYSTELGGH RHMASRHLGR
GVTEQQRSRW VALLLDTADQ VGLPADPEFR GVLAYYLEWG TRMALIYSGP NPPPLPETPM
PRWDWGITPP YRG
//