ID A0A4D9ETA0_9SAUR Unreviewed; 881 AA.
AC A0A4D9ETA0;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000256|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03050};
GN Name=MOCOS {ECO:0000256|HAMAP-Rule:MF_03050};
GN ORFNames=DR999_PMT08091 {ECO:0000313|EMBL:TFK08974.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK08974.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK08974.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK08974.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK08974.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK08974.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK08974.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK08974.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum
CC is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase
CC (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and
CC 1 sulfur atom in active form. {ECO:0000256|HAMAP-Rule:MF_03050}.
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:0000256|ARBA:ARBA00029322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645;
CC Evidence={ECO:0000256|ARBA:ARBA00029322};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine +
CC thio-Mo-molybdopterin; Xref=Rhea:RHEA:42636, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:71302, ChEBI:CHEBI:82685; EC=2.8.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03050};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03050}.
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:TFK08974.1}.
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DR EMBL; QXTE01000060; TFK08974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4D9ETA0; -.
DR STRING; 55544.A0A4D9ETA0; -.
DR Proteomes; UP000297703; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_03050; MOCOS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR028886; MoCo_sulfurase.
DR InterPro; IPR005303; MOCOS_middle.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_03050};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03050};
KW Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 707..862
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 434
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 881 AA; 98067 MW; 6FEFA15B3AEE6718 CRC64;
MAGQAQSRAE LQQQAAPPWG ELLSFQYFQR LCPPGAGYGY SGGSMQGMRE SEFRRLGGMT
YLDHAGTALF PQSLLKEFTD DLSKNIYGNP HSQNISSKLT YDTIEHVRYR ILQYFNTTAE
DYTIIFTSGS TAALKLVAET FPWMPEGSGH PSSRFCYLTD SHTSVVGMRG ITAAMNVLSV
PVKPKEILLS EKNRVPAEEQ NCMTPHIFCY PAQSNFSGIK YPLSWIQEIK SGKLCPIKTP
GKWFVLLDAA SYVSTSPLDL TVHQPDFIPI SFYKIFGFPT GLGALLVNNQ IAPFLRKSYF
GGGTAAGYLA GEEFYSPRPS VAERFEDGTV SFLDIIALKH GFDALERLTG GMENIKHHTF
ALSHYTYTVL STLKYANGAP IVRIYSDSDF SSPDVQGPII NFNVLDENGD VIGYSQVDKI
ASLYNIHLRT GCFCNTGACQ QHLSLSNEDV KRNLQAGHVC GDDIDMIDGH PTGSVRISFG
YMSTFEDAQT FLKFIIATRL SESDCKFPSQ TTTRETITQS VESPIQNDHT ANNNANKYSL
KTIISDTGHW NNSSAALKTP ETSRAVVSES AIPVYRSGSK PITVTNIYLY PIKSCSAFEV
SEWPVGNQGL LYDRSWMVVN QNGVCISQKQ EHRLCLVHPI INLEQKIMVI KAEGMDPISV
PLEENTGREI QIGQSKVCAH RVQTYDCGER IAEWFSELLG RQCRLIRQSS DFKRNANQKH
EKGQATTVSL SLVNEAQYLL INTASILQLK EQITERLKEP LQTEELIQRF RANIVISATE
SFEEEKWAEI SIGALCFQVV GPCNRCQIIC IDPQTGQRNK EFLQTLSSTR GRKTNFGIYL
MNQSLCSSLP NTLSVGSQVF PVLKEDREIQ SPLSNEEKTS G
//
