MOP_MEGGA
ID MOP_MEGGA Reviewed; 907 AA.
AC Q46509;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Aldehyde oxidoreductase;
DE EC=1.2.99.7;
DE AltName: Full=Molybdenum iron sulfur protein;
GN Name=mop;
OS Megalodesulfovibrio gigas (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8143744; DOI=10.1111/j.1432-1033.1994.tb18693.x;
RA Thoenes U., Flores O.L., Neves A., Devreese B., van Beeumen J.J., Huber R.,
RA Romao M.J., Legall J., Moura J.J.G., Rodriges-Pousada C.;
RT "Molecular cloning and sequence analysis of the gene of the molybdenum-
RT containing aldehyde oxido-reductase of Desulfovibrio gigas. The deduced
RT amino acid sequence shows similarity to xanthine dehydrogenase.";
RL Eur. J. Biochem. 220:901-910(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=7502041; DOI=10.1126/science.270.5239.1170;
RA Romao M.J., Archer M., Moura I., Moura J.J.G., LeGall J., Engh R.,
RA Schneider M., Hof P., Huber R.;
RT "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase
RT from D. gigas.";
RL Science 270:1170-1176(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8799115; DOI=10.1073/pnas.93.17.8846;
RA Huber R., Hof P., Duarte R.O., Moura J.J.G., Moura I., Liu M.-Y.,
RA LeGall J., Hille R., Archer M., Romao M.J.;
RT "A structure-based catalytic mechanism for the xanthine oxidase family of
RT molybdenum enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8846-8851(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS).
RX PubMed=11713686; DOI=10.1007/s007750100255;
RA Rebelo J.M., Dias J.M., Huber R., Moura J.J., Romao M.J.;
RT "Structure refinement of the aldehyde oxidoreductase from Desulfovibrio
RT gigas (MOP) at 1.28 A.";
RL J. Biol. Inorg. Chem. 6:791-800(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + an aldehyde + H2O = a carboxylate + AH2 + H(+);
CC Xref=Rhea:RHEA:56856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29067; EC=1.2.99.7;
CC -!- COFACTOR:
CC Name=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308;
CC Note=Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor
CC per subunit.;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 2 [2Fe-2S] clusters per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X77222; CAA54439.1; -; Genomic_DNA.
DR PIR; A57429; A57429.
DR PDB; 1SIJ; X-ray; 2.30 A; A=1-907.
DR PDB; 1VLB; X-ray; 1.28 A; A=1-907.
DR PDB; 3FAH; X-ray; 1.72 A; A=1-907.
DR PDB; 3FC4; X-ray; 1.79 A; A=1-907.
DR PDB; 3L4P; X-ray; 1.45 A; A=1-907.
DR PDB; 4C7Y; X-ray; 1.57 A; A=1-907.
DR PDB; 4C7Z; X-ray; 1.55 A; A=1-907.
DR PDB; 4C80; X-ray; 1.50 A; A=1-907.
DR PDB; 4US8; X-ray; 1.49 A; A=1-907.
DR PDB; 4US9; X-ray; 1.40 A; A=1-907.
DR PDB; 4USA; X-ray; 1.13 A; A=1-907.
DR PDBsum; 1SIJ; -.
DR PDBsum; 1VLB; -.
DR PDBsum; 3FAH; -.
DR PDBsum; 3FC4; -.
DR PDBsum; 3L4P; -.
DR PDBsum; 4C7Y; -.
DR PDBsum; 4C7Z; -.
DR PDBsum; 4C80; -.
DR PDBsum; 4US8; -.
DR PDBsum; 4US9; -.
DR PDBsum; 4USA; -.
DR AlphaFoldDB; Q46509; -.
DR SMR; Q46509; -.
DR DrugBank; DB02137; Molybdenum cofactor.
DR PRIDE; Q46509; -.
DR OMA; CTHNPLG; -.
DR BRENDA; 1.2.99.7; 1907.
DR SABIO-RK; Q46509; -.
DR EvolutionaryTrace; Q46509; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0033727; F:aldehyde dehydrogenase (FAD-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR11908; PTHR11908; 2.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; NAD; Oxidoreductase.
FT CHAIN 1..907
FT /note="Aldehyde oxidoreductase"
FT /id="PRO_0000166102"
FT DOMAIN 2..79
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:7502041"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:7502041"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:7502041"
FT BINDING 60
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:7502041"
FT BINDING 100
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:7502041"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:7502041"
FT BINDING 137
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:7502041"
FT BINDING 139
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:7502041"
FT BINDING 653
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT BINDING 869
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 216..226
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 330..341
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 351..360
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 392..403
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 463..471
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 477..487
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 495..505
FT /evidence="ECO:0007829|PDB:4USA"
FT TURN 506..509
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:4USA"
FT TURN 533..536
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 537..555
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 559..566
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 585..606
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 609..626
FT /evidence="ECO:0007829|PDB:4USA"
FT TURN 627..629
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 631..638
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 657..669
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:4USA"
FT TURN 686..688
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 700..719
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 729..734
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 740..746
FT /evidence="ECO:0007829|PDB:4USA"
FT TURN 755..757
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 766..778
FT /evidence="ECO:0007829|PDB:4USA"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 784..794
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 801..820
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:4USA"
FT TURN 833..837
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 841..843
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 848..852
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 858..860
FT /evidence="ECO:0007829|PDB:1SIJ"
FT HELIX 861..863
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 870..872
FT /evidence="ECO:0007829|PDB:4USA"
FT HELIX 875..887
FT /evidence="ECO:0007829|PDB:4USA"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:1SIJ"
FT HELIX 898..906
FT /evidence="ECO:0007829|PDB:4USA"
SQ SEQUENCE 907 AA; 97035 MW; 898E7EEF708A64DF CRC64;
MIQKVITVNG IEQNLFVDAE ALLSDVLRQQ LGLTGVKVGC EQGQCGACSV ILDGKVVRAC
VTKMKRVADG AQITTIEGVG QPENLHPLQK AWVLHGGAQC GFCSPGFIVS AKGLLDTNAD
PSREDVRDWF QKHRNACRCT GYKPLVDAVM DAAAVINGKK PETDLEFKMP ADGRIWGSKY
PRPTAVAKVT GTLDYGADLG LKMPAGTLHL AMVQAKVSHA NIKGIDTSEA LTMPGVHSVI
THKDVKGKNR ITGLITFPTN KGDGWDRPIL CDEKVFQYGD CIALVCADSE ANARAAAEKV
KVDLEELPAY MSGPAAAAED AIEIHPGTPN VYFEQPIVKG EDTGPIFASA DVTVEGDFYV
GRQPHMPIEP DVAFAYMGDD GKCYIHSKSI GVHLHLYMIA PGVGLEPDQL VLVANPMGGT
FGYKFSPTSE ALVAVAAMAT GRPVHLRYNY QQQQQYTGKR SPWEMNVKFA AKKDGTLLAM
ESDWLVDHGP YSEFGDLLTL RGAQFIGAGY NIPNIRGLGR TVATNHVWGS AFRGYGAPQS
MFASECLMDM LAEKLGMDPL ELRYKNAYRP GDTNPTGQEP EVFSLPDMID QLRPKYQAAL
EKAQKESTAT HKKGVGISIG VYGSGLDGPD ASEAWAELNA DGTITVHTAW EDHGQGADIG
CVGTAHEALR PMGVAPEKIK FTWPNTATTP NSGPSGGSRQ QVMTGNAIRV ACENLLKACE
KPGGGYYTYD ELKAADKPTK ITGNWTASGA THCDAVTGLG KPFVVYMYGV FMAEVTVDVA
TGQTTVDGMT LMADLGSLCN QLATDGQIYG GLAQGIGLAL SEDFEDIKKH ATLVGAGFPF
IKQIPDKLDI VYVNHPRPDG PFGASGVGEL PLTSPHAAII NAIKSATGVR IYRLPAYPEK
VLEALKA
