DCML_HYDPS
ID DCML_HYDPS Reviewed; 803 AA.
AC P19913; Q9RBR9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Carbon monoxide dehydrogenase large chain;
DE Short=CO dehydrogenase subunit L;
DE Short=CO-DH L;
DE EC=1.2.5.3 {ECO:0000250|UniProtKB:P19919};
GN Name=cutL;
OS Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=47421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], COFACTOR, AND SUBUNIT.
RX PubMed=10482497; DOI=10.1128/jb.181.18.5581-5590.1999;
RA Kang B.S., Kim Y.M.;
RT "Cloning and molecular characterization of the genes for carbon monoxide
RT dehydrogenase and localization of molybdopterin, flavin adenine
RT dinucleotide, and iron-sulfur centers in the enzyme of Hydrogenophaga
RT pseudoflava.";
RL J. Bacteriol. 181:5581-5590(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-9.
RX PubMed=2818128; DOI=10.1007/bf00425170;
RA Kraut M., Hugendieck I., Herwig S., Meyer O.;
RT "Homology and distribution of CO dehydrogenase structural genes in
RT carboxydotrophic bacteria.";
RL Arch. Microbiol. 152:335-341(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND HYDROXYLATION AT ARG-384.
RX PubMed=10966817; DOI=10.1006/jmbi.2000.4023;
RA Haenzelmann P., Dobbek H., Gremer L., Huber R., Meyer O.;
RT "The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on
RT the crystallographic structure of the seleno-molybdo-iron-sulfur
RT flavoenzyme carbon monoxide dehydrogenase.";
RL J. Mol. Biol. 301:1221-1235(2000).
RN [4]
RP REVIEW.
RX PubMed=11076018; DOI=10.1515/bc.2000.108;
RA Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., Gnida M.,
RA Meyer-Klaucke W., Huber R.;
RT "The role of Se, Mo and Fe in the structure and function of carbon monoxide
RT dehydrogenase.";
RL Biol. Chem. 381:865-876(2000).
CC -!- FUNCTION: Catalyzes the oxidation of carbon monoxide to carbon dioxide.
CC {ECO:0000250|UniProtKB:P19919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + CO + H2O = a quinol + CO2; Xref=Rhea:RHEA:48880,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.2.5.3;
CC Evidence={ECO:0000250|UniProtKB:P19919};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Note=Binds 1 Cu(+) ion per subunit.;
CC -!- COFACTOR:
CC Name=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308;
CC Evidence={ECO:0000269|PubMed:10482497};
CC Note=Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor
CC per subunit. {ECO:0000269|PubMed:10482497};
CC -!- SUBUNIT: Dimer of heterotrimers. Each heterotrimer consists of a large,
CC a medium and a small subunit. {ECO:0000269|PubMed:10482497}.
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DR EMBL; U80806; AAD00363.1; -; Genomic_DNA.
DR PIR; PL0139; PL0139.
DR PDB; 1FFU; X-ray; 2.35 A; B/E=1-803.
DR PDB; 1FFV; X-ray; 2.25 A; B/E=1-803.
DR PDBsum; 1FFU; -.
DR PDBsum; 1FFV; -.
DR AlphaFoldDB; P19913; -.
DR SMR; P19913; -.
DR BRENDA; 1.2.5.3; 2729.
DR EvolutionaryTrace; P19913; -.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro.
DR GO; GO:0008805; F:carbon-monoxide oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
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; IPR012780; CO_Mo_DH_lsu.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR TIGRFAMs; TIGR02416; CO_dehy_Mo_lg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Hydroxylation;
KW Metal-binding; Molybdenum; Oxidoreductase.
FT CHAIN 1..803
FT /note="Carbon monoxide dehydrogenase large chain"
FT /id="PRO_0000079809"
FT BINDING 385
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT BINDING 757
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT MOD_RES 384
FT /note="4-hydroxyarginine"
FT /evidence="ECO:0000269|PubMed:10966817"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1FFU"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 325..335
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 389..407
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 453..465
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 470..481
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 526..538
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 566..592
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 604..611
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 619..628
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 636..644
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 653..663
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 669..679
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 686..705
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 737..740
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 758..775
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 789..798
FT /evidence="ECO:0007829|PDB:1FFV"
SQ SEQUENCE 803 AA; 87229 MW; 3CD5FE205DBE0712 CRC64;
MNAPVQDAEA RELALAGMRP RACAKEDARF IQGKGNYVDD IKMPGMLHMD IVRAPIAHGR
IKKIHKDAAL AMPGVHAVLT AEDLKPLKLH WMPTLAGDVA AVLADEKVHF QMQEVAIVIA
DDRYIAADAV EAVKVEYDEL PVVIDPIDAL KPDAPVLRED LAGKTSGAHG PREHHNHIFT
WGAGDKAATD AVFANAPVTV SQHMYYPRVH PCPLETCGCV ASFDPIKGDL TTYITSQAPH
VVRTVVSMLS GIPESKVRIV SPDIGGGFGN KVGIYPGYVC AIVASIVLGR PVKWVEDRVE
NISTTAFARD YHMDGELAAT PDGKILGLRV NVVADHGAFD ACADPTKFPA GLFHICSGSY
DIPRAHCSVK GVYTNKAPGG VAYRCSFRVT EAVYLIERMV DVLAQKLNMD KAEIRAKNFI
RKEQFPYTTQ FGFEYDSGDY HTALKKVLDA VDYPAWRAEQ AARRADPNSP TLMGIGLVTF
TEVVGAGPSK MCDILGVGMF DSCEIRIHPT GSAIARMGTI TQGQGHQTTY AQIIATELGI
PSEVIQVEEG DTSTAPYGLG TYGSRSTPVA GAAIALAARK IHAKARKIAA HMLEVNENDL
DWEVDRFKVK GDDSKFKTMA DIAWQAYHQP PAGLEPGLEA VHYYDPPNFT YPFGIYLCVV
DIDRATGETK VRRFYALDDC GTRINPMIIE GQIHGGLTEG YAVAMGQQMP FDAQGNLLGN
TLMDYFLPTA VETPHWETDH TVTPSPHHPI GAKGVAESPH VGSIPTFTAA VVDAFAHVGV
THLDMPHTSY RVWKSLKEHN LAL
