ID A0A1B9DAH7_MYCMA Unreviewed; 454 AA.
AC A0A1B9DAH7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cytochrome {ECO:0000313|EMBL:OCB57814.1};
GN ORFNames=A5677_01700 {ECO:0000313|EMBL:OCB57814.1};
OS Mycobacterium malmoense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1780 {ECO:0000313|EMBL:OCB57814.1, ECO:0000313|Proteomes:UP000092683};
RN [1] {ECO:0000313|EMBL:OCB57814.1, ECO:0000313|Proteomes:UP000092683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3012 {ECO:0000313|EMBL:OCB57814.1,
RC ECO:0000313|Proteomes:UP000092683};
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|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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:OCB57814.1}.
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DR EMBL; MBEE01000079; OCB57814.1; -; Genomic_DNA.
DR RefSeq; WP_065480094.1; NZ_MBEE01000079.1.
DR AlphaFoldDB; A0A1B9DAH7; -.
DR OrthoDB; 3209493at2; -.
DR Proteomes; UP000092683; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 51013 MW; E812F6E2D1930A67 CRC64;
MSVGDAVGGS DRKKKRYQFE RHSPEYRSNF KAITEEMHAK CPMAWSDTYG GHWVAAGSHE
VFELARCPAV SNDHDVNNER RGYKGISIPT ASRINGVRGG ILEMDDPEHR IYRNVLNPYL
SPAAVKRWKP FIDDVTRACL DEKIEKGQID FVDDLANVVP AVLTLAMLGI PLKNWQMYSE
PTHAAVYTPE HSPDIQRVTE MHRQMGLDLV NNMIEIRQNP RPGIVNALLE MRIDGEPAPD
LEILGNLGLV IGGGFDTTTA LTAHSLEWLS EHPDQRELLS TQRGTLLDPA TEEFLRYFTP
APGDGRTFSD DVELDGTQFK EGERLWISWA MANRDPAVFK DPDEIVLDRK GNRHFSFGLG
VHRCIGSNVA RTVFKSMLTA VLDRMPDYHC DPEGTIHYET IGVIQGMRKL PAGFTPGRKI
GAGLDETLEK LQRICDEQEL ARPITERKEE AVID
//