ID DHM1_METOR Reviewed; 626 AA. AC P15279; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 16-JUN-2009, entry version 75. DE RecName: Full=Methanol dehydrogenase subunit 1; DE EC=1.1.99.8; DE AltName: Full=MDH large subunit alpha; DE AltName: Full=MEDH; DE Flags: Precursor; GN Name=moxF; OS Methylobacterium organophilum XX. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=410; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-43. RC STRAIN=ATCC 27886 / DSM 760 / IFO 15689 / JCM 2833 / NCIB 11278; RX MEDLINE=89008094; PubMed=2459109; RA Machlin S.M., Hanson R.S.; RT "Nucleotide sequence and transcriptional start site of the RT Methylobacterium organophilum XX methanol dehydrogenase structural RT gene."; RL J. Bacteriol. 170:4739-4747(1988). CC -!- CATALYTIC ACTIVITY: A primary alcohol + acceptor = an aldehyde + CC reduced acceptor. CC -!- COFACTOR: Binds 1 PQQ group per subunit. PQQ is inserted between CC disulfide Cys-130-Cys-131 and the indole ring of Trp-270 (By CC similarity). CC -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity). CC -!- SUBUNIT: Heterotetramer composed of 2 alpha and 2 beta subunits. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane CC protein; Periplasmic side. Note=Periplasmic, but associated with CC inner membrane. CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M22629; AAA50289.1; -; Genomic_DNA. DR HSSP; P16027; 1H4J. DR SMR; P15279; 28-622. DR BioCyc; MetaCyc:MON-3927; -. DR BRENDA; 1.1.99.8; 190843. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0018468; F:alcohol dehydrogenase (acceptor) activity; IEA:EC. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR019556; PQQ-dependent_C. DR InterPro; IPR019551; PQQ-dependent_N. DR InterPro; IPR018391; PQQ_beta_propeller_repeat. DR InterPro; IPR017512; PQQ_MeOH/EtOH_DH. DR InterPro; IPR002372; PQQ_repeat. DR InterPro; IPR011047; Quino_AlcDH-like. DR InterPro; IPR001479; Quinoprotein_DH_CS. DR Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 1. DR Pfam; PF01011; PQQ; 5. DR Pfam; PF10535; PQQ_C; 1. DR Pfam; PF10527; PQQ_N; 1. DR SMART; SM00564; PQQ; 3. DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1. DR PROSITE; PS00363; BACTERIAL_PQQ_1; 1. DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1. PE 1: Evidence at protein level; KW Calcium; Cell inner membrane; Cell membrane; KW Direct protein sequencing; Disulfide bond; Membrane; Metal-binding; KW Methanol utilization; Oxidoreductase; PQQ; Signal. FT SIGNAL 1 27 FT CHAIN 28 626 Methanol dehydrogenase subunit 1. FT /FTId=PRO_0000025567. FT ACT_SITE 330 330 Proton acceptor (By similarity). FT METAL 204 204 Calcium (By similarity). FT METAL 288 288 Calcium (By similarity). FT DISULFID 130 131 By similarity. FT DISULFID 413 442 By similarity. SQ SEQUENCE 626 AA; 68677 MW; 8768F6B8371E5DFF CRC64; MSRFVTSVSA LAMLALAPAA LSSVAYANDK LVELSKSDDN WVMPGKNYDS NNYSELKQVN KSNVKQLRPA WTFSTGLLNG HEGAPLVVDG KMYVHTSFPN NTFALDLDDP GHILWQDKPK QNPAARAVAC CDLVNRGLAY WPGDGKTPAL ILKTQLDRHV VALNAETGET VWKVENSDIK VGSTLTIAPY VVKDKVIIGS SGAELGVRGY LTAYDVKTGG QVWRAYATGP DKDLLLADDF NVKNAHYGQK GLGTATWEGD AWKIGGGTNW GWYAYDPGTN LIYFGTGNPA PWNETMRPGD NKWTMTIFGR DADTGEAKFG YQKTPHDEWD YAGVNVMMPS EQKDKDGKTR KLLTHPDRNG IVYTLDRTDG ALVSANKLDD TVNVFKTVDL KTGQPVRDPE YGTRMDHLAK DVCPSAMGYH NQGHDSYDPK RELFFMGINH ICMDWEPFML PYRAGQFFVG ATLNMYPGPK GDRQNYEGLG QIKAYNAITG SYKWEKMERF AVWGGTLATA GDLVFYGTLD GYLKARDSDT GDLLWKFKIP SGAIGYPMTY THKGTQYVAI YYGVGGWPGV GLVFDLADPT AGLGAVGAFK KLANYTQQGG GVIVFSLDGK GPYDDPNVGE WKSASK //