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Database: UniProt
Entry: K5B9X3_MYCHD
LinkDB: K5B9X3_MYCHD
Original site: K5B9X3_MYCHD 
ID   K5B9X3_MYCHD            Unreviewed;       308 AA.
AC   K5B9X3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Ring hydroxylating alpha subunit family protein {ECO:0000313|EMBL:EKF21240.1};
DE   Flags: Fragment;
GN   ORFNames=C731_4826 {ECO:0000313|EMBL:EKF21240.1};
OS   Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS   3849) (Mycobacterium hassiacum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF21240.1, ECO:0000313|Proteomes:UP000006265};
RN   [1] {ECO:0000313|EMBL:EKF21240.1, ECO:0000313|Proteomes:UP000006265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC   {ECO:0000313|Proteomes:UP000006265};
RX   PubMed=23209251; DOI=10.1128/JB.01880-12;
RA   Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA   Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT   "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT   heat-stable mycobacterial proteins.";
RL   J. Bacteriol. 194:7010-7011(2012).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
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:EKF21240.1}.
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DR   EMBL; AMRA01000155; EKF21240.1; -; Genomic_DNA.
DR   RefSeq; WP_005632599.1; NZ_AMRA01000155.1.
DR   AlphaFoldDB; K5B9X3; -.
DR   STRING; 1122247.GCA_000379865_00974; -.
DR   PATRIC; fig|1122247.3.peg.4626; -.
DR   eggNOG; COG4638; Bacteria.
DR   Proteomes; UP000006265; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00680; RHO_alpha_C; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43756:SF5; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00022714};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022714};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006265}.
FT   DOMAIN          70..292
FT                   /note="Aromatic-ring-hydroxylating dioxygenase alpha
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00848"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKF21240.1"
SQ   SEQUENCE   308 AA;  34583 MW;  06BD2CD887762FCA CRC64;
     YNLDGSLHSP TRRDLLLDFD PDSCRLPAVQ CEVWEGFIFI NLDPHNTEPL RSYLGELAHG
     LEGYPFAGPH QVYRFRVELQ CNWKIFLDGF AESYHGPYLH ASSFGALTAE AREAFDKPNP
     YTDALAYRLV GPHRMFSFSG EPSQRTPYSK PIECVMEAGA AGPWNKRTDR GPMPPGINPT
     RSERYGFDSY QFFPNFVLIF GASGFSTHAH WPTGPHSHLF EVEMFYDPPT SHKERLGQEL
     TVTFLNDIIL EDASPAEGLQ AMLNSGALTH FHFNDEEILL RHFHKVVADY VAAGEGAAGE
     RAGVESSR
//
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