MARC1_XENLA
ID MARC1_XENLA Reviewed; 343 AA.
AC Q5U534;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) 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 1-44 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; BC084850; AAH84850.1; -; mRNA.
DR RefSeq; NP_001088512.1; NM_001095043.2.
DR AlphaFoldDB; Q5U534; -.
DR SMR; Q5U534; -.
DR DNASU; 495382; -.
DR GeneID; 495382; -.
DR KEGG; xla:495382; -.
DR CTD; 495382; -.
DR Xenbase; XB-GENE-5823412; mtarc1.S.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 495382; Expressed in liver and 20 other tissues.
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; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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..343
FT /note="Mitochondrial amidoxime-reducing component 1"
FT /id="PRO_0000273338"
FT TOPO_DOM 1..25
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 26..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 181..339
FT /note="MOSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00670"
FT REGION 95..186
FT /note="MOSC N-terminal region"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 69
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 70
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 94
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 215
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 242
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 276
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
FT BINDING 277
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 321
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q5VT66"
SQ SEQUENCE 343 AA; 38221 MW; 7BBEBF378A392AEB CRC64;
MSNTVFSGAV GPLRAAALSI SRHRLPLLCA AGLGLTAVAS WMWWRKRQGE AEDLQQVGIV
SQLLIYPVKS CRAVPVQEAE CSALGLKSGH LEDRHWLVVT EEGNMVTARQ EPRMVLISAT
FCGNTLCLNG PEMQEVQIPL PLPKSNRVLD CRVFGQDIQG RDSGEQASEW LATYFQSSQP
YRLVHFEADV MRPRQSKKKE KLFRDKDVIA YPDASPIMLL SETSMEALNS RLEQPVSLAN
FRPCIVASGC EAFAEDDWDD VRLGATRLKR VMACGRCVLT TVNPNSGVIT RKEPLDTLRT
FRQSDSSLKE VYKNAPLFGQ YYGVEQTGII RVGDPVYRVT RKG
