MARC1_DANRE
ID MARC1_DANRE Reviewed; 325 AA.
AC Q58EJ9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Mitochondrial amidoxime-reducing component 1 {ECO:0000250|UniProtKB:Q5VT66};
DE Short=mARC1 {ECO:0000250|UniProtKB:Q5VT66};
DE EC=1.7.-.- {ECO:0000250|UniProtKB:Q5VT66};
GN Name=mtarc1; Synonyms=marc1; ORFNames=zgc:110783;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of N-oxygenated molecules, acting as
CC a counterpart of cytochrome P450 and flavin-containing monooxygenases
CC in metabolic cycles. As a component of prodrug-converting system,
CC reduces a multitude of N-hydroxylated prodrugs particularly amidoximes,
CC leading to increased drug bioavailability. May be involved in
CC mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating
CC endogenous nitric oxide levels and biosynthesis. Postulated to cleave
CC the N-OH bond of N-hydroxylated substrates in concert with electron
CC transfer from NADH to cytochrome b5 reductase then to cytochrome b5,
CC the ultimate electron donor that primes the active site for substrate
CC reduction. {ECO:0000250|UniProtKB:Q5VT66}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N(omega)-hydroxy-L-
CC arginine = 2 Fe(III)-[cytochrome b5] + H2O + L-arginine;
CC Xref=Rhea:RHEA:61644, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:32682, ChEBI:CHEBI:60107;
CC Evidence={ECO:0000250|UniProtKB:Q5VT66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645;
CC Evidence={ECO:0000250|UniProtKB:Q5VT66};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:Q5VT66};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:Q5VT66};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q5VT66}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q5VT66}. Membrane
CC {ECO:0000250|UniProtKB:Q5VT66}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q5VT66}. Note=Mitochondrial import is mediated
CC by AA 1-36 and requires ATP. {ECO:0000250|UniProtKB:Q5VT66}.
CC -!- DOMAIN: Comprises two structural domains, the molybdenum cofactor/Moco
CC sulfurase C-terminal (MOSC) domain and the MOSC N-terminal region,
CC forming a cleft that accommodates Moco. The MOSC domain, which contains
CC a large seven-stranded mostly antiparallel beta-barrel, engages
CC multiple interactions with Moco both pterin ring and phosphate group,
CC allowing for a tight coordination of Moco within the core of the
CC enzyme. {ECO:0000250|UniProtKB:Q5VT66}.
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DR EMBL; BC091870; AAH91870.1; -; mRNA.
DR AlphaFoldDB; Q58EJ9; -.
DR SMR; Q58EJ9; -.
DR STRING; 7955.ENSDARP00000094269; -.
DR PaxDb; Q58EJ9; -.
DR ZFIN; ZDB-GENE-050327-95; marc1.
DR eggNOG; KOG2362; Eukaryota.
DR InParanoid; Q58EJ9; -.
DR PhylomeDB; Q58EJ9; -.
DR Reactome; R-DRE-211945; Phase I - Functionalization of compounds.
DR PRO; PR:Q58EJ9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IBA:GO_Central.
DR GO; GO:0008940; F:nitrate reductase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0042126; P:nitrate metabolic process; IBA:GO_Central.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR005303; MOSC_N.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF50800; SSF50800; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 2: Evidence at transcript level;
KW Lipoprotein; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Molybdenum; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..325
FT /note="Mitochondrial amidoxime-reducing component 1"
FT /id="PRO_0000273337"
FT TOPO_DOM 1..16
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 17..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 179..323
FT /note="MOSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00670"
FT REGION 85..175
FT /note="MOSC N-terminal region"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 59
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 60
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 84
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 230
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 264
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 265
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 305
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
SQ SEQUENCE 325 AA; 36716 MW; CBB1A2111C408340 CRC64;
MDLKEAFATI FDQNRKVALY AAGTTVAVLG LGLVFKYMRR EEKLTRVGVV TKLLVHPLKS
GKAVSVEAAE CLRMGLKYGE LRDRHWLVIT EDGHMVTGRQ QPRLVLVSLT CEGGHVSLNG
PQMEELKFPL NNSSDLVVDC RVFSVDVQGR DCGDKVSEWL TRFLEADKPV RLVHYEPDLK
PQRPHEKEPL FPKDDEVAYP DAAPVMLMTE ASVGDLNSRL DKDLSVFQFR PSIVVSDCEA
FTEDTWDHIR IGEVELKRVI GCGRCLFTTV DPETGVFSRK EPLETLKTYR MTDPKQKTSP
ILGQYYTVRK TGVLHVGEPV YKITY
