ID A0A2T7PQZ3_POMCA Unreviewed; 764 AA.
AC A0A2T7PQZ3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=C0Q70_02804 {ECO:0000313|EMBL:PVD35835.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD35835.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD35835.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD35835.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD35835.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) 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=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:PVD35835.1}.
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DR EMBL; PZQS01000002; PVD35835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PQZ3; -.
DR STRING; 400727.A0A2T7PQZ3; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg2.
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 PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR Pfam; PF00266; Aminotran_5; 2.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal 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:UP000245119};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 623..764
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 95..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 410
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 764 AA; 84044 MW; 73B0CED6CC2A85F7 CRC64;
MTKGLTYVDH AGATLYAKSQ MTAVHEDLVS HLYGNPHSSS ASSRFCTDAI DQTRFRILRF
FNTDPDTYSV VFTSGCTGAL KLVAETFNFS RPRQALAGRR HSRGKPGRCE PPSGTSRYRS
DYCQGYFCYL QDNHTSVQGM RELAAAGRCR GILCLTEAEV QQGLADESLV WGSLEAPSAG
GSSLFVFPGQ SNYSGRKYPL EWVGWAQKGD LAFQRSLVAE KWFVVLDAAC LVSTSPLDLS
LVRPDFVTLS FYKMFGFPTG LGALLVRNSS AWVLEKKYFG GGTVAASSAR ERFCVLRAGV
CDRRHVALSG HHRLNHGFRA LDSLGGGMEA ISAHTFTIAH FFATNLSRLH HSNGTAIAEI
YSADGFQDRS KQGAIVNFNL RRANGDYIGF AEVDKLAQLH DIHLRTGCFC NIGACQMFLN
ITSETIQDNL KAGHVCGDDV DLVNGRPTGS VRVSFGYMSS LTDAIRCLNF MVDCFLDTIV
SRPLPEHSAD MACSEKVRRL TDIFLYPIKS CGAFRVSEWQ TGPRGLLYDR TWMVVSDNGI
ALGQKREPRL CLLAPVIHLD SGKLELSFPG TESCYIGLDT YETDEVNNTS ICTNKICNDK
VNTVDCGEAV AQWLCETLER PGLRLLRQLH DDSRHSKRKD VAAGDTAPDA ATSPGLSLAN
EAQFLLISRE SVRSLQKKLV EQQDDDLREV KGQKSGAQAF SEQNLVQRFR ANLVIDGGLP
FDEESWTSVS CGDVALVVYF GVYLRSAESD VEQVLRVGSE VFVA
//
