ID A0A0D2F7S1_9EURO Unreviewed; 809 AA.
AC A0A0D2F7S1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Choline monooxygenase, chloroplastic {ECO:0000256|ARBA:ARBA00014931};
DE EC=1.14.15.7 {ECO:0000256|ARBA:ARBA00012763};
GN ORFNames=PV05_04767 {ECO:0000313|EMBL:KIW56079.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW56079.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW56079.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW56079.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step of the osmoprotectant glycine
CC betaine synthesis. {ECO:0000256|ARBA:ARBA00002149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC betaine aldehyde hydrate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:17769, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15870, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738; EC=1.14.15.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001883};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine aldehyde from choline (monooxygenase route):
CC step 1/1. {ECO:0000256|ARBA:ARBA00004866}.
CC -!- SIMILARITY: Belongs to the choline monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010848}.
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DR EMBL; KN847319; KIW56079.1; -; Genomic_DNA.
DR RefSeq; XP_013316663.1; XM_013461209.1.
DR AlphaFoldDB; A0A0D2F7S1; -.
DR STRING; 348802.A0A0D2F7S1; -.
DR GeneID; 25326675; -.
DR HOGENOM; CLU_348516_0_0_1; -.
DR OrthoDB; 1946667at2759; -.
DR UniPathway; UPA00529; UER00430.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0019133; F:choline monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR CDD; cd03469; Rieske_RO_Alpha_N; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR021858; Fun_TF.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43756:SF5; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF11951; Fungal_trans_2; 2.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 134..219
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 526..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 91846 MW; 66CA7CB748B6E349 CRC64;
MVFDVKPKTE KFKVQNLPGV PEHVYFTDCL GSRDEQVQNP IVGSWFRIEQ GPPTAPPKYE
YDEVGIVIEG IITLQDEDDG TKNTVTAEDV FVIHRVKSNE STPGVGATLP ASWYSTRGIY
ECERRAIFAR RWLLVSHELR FQAPGAYAKF TIAGYPFFII RDCKGNLNAF LNVCRHRAFP
VVLQDSGNAS ILACKYHGWS YGLNGNLAKA PKFAGVEGFD ESQHGLFRVH LKVDERKFVW
VNLDSAKVPE VSWEESFQHV DLQERLGAFD MKRYRYDHSC DQDFEEMGRF FKQVEREDKY
LCTHAQRNIN AGGYVSGPLH PHNEKGVLHF QSLIKTCLVE HREKEKSLGR EIAPAKRSPK
SSVTEEEELF YRNEFRTMAV SRTKESLLVF SLCRYLTAVF LNSSVFGTSS ILVVQDTQTD
LLHRLQHEVA QLDTSKQAKV EEVLMAVIMF GLSTNWDCSN TPSIFHYNAA VRIYRHVYQD
SKSNACRSDH QDFFVQSLIY WWMGLCFVTD TRQDCLLEPP FGDLSAAGTS SESTQSDRRI
PHPLTGVSPE AQKLLGDVGS LEARRLEEEA LSMDSPRTHN FLDLGDPDTP LEDLVRTAEV
YRLSALILLY RTFPDLLNVR LRLAEDASSD SQQAEQRRLL WLTALATHAL QIVCLNAPCS
GTRSIESILL VIIAGELRKP PSSESAVLQL YHQDDTTNFN SLLEETPPAL AVMMDSVDQF
AALRGFSQQG LIDLGFDGSL RDALGLDHVA EARTTILRRL QSIREILPYR SLEIVEEIVL
TTWNMGDQEK SEVFWMDIMI EKGWRFLLV
//