MAUM_PARDP
ID MAUM_PARDP Reviewed; 224 AA.
AC Q51659; A1BBA4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Methylamine utilization ferredoxin-type protein MauM;
DE Flags: Precursor;
GN Name=mauM; OrderedLocusNames=Pden_4737;
OS Paracoccus denitrificans (strain Pd 1222).
OG Plasmid pPD1222.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7601147; DOI=10.1111/j.1432-1033.1995.tb20629.x;
RA van der Palen C.J., Slotboom D.J., Jongejan L., Reijnders W.N., Harms N.,
RA Duine J.A., van Spanning R.J.;
RT "Mutational analysis of mau genes involved in methylamine metabolism in
RT Paracoccus denitrificans.";
RL Eur. J. Biochem. 230:860-871(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of plasmid 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in electron transfer. {ECO:0000305}.
CC -!- PATHWAY: One-carbon metabolism; methylamine degradation.
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DR EMBL; U15028; AAA86468.1; -; Genomic_DNA.
DR EMBL; CP000491; ABL72798.1; -; Genomic_DNA.
DR PIR; S65960; S65960.
DR AlphaFoldDB; Q51659; -.
DR STRING; 318586.Pden_4737; -.
DR PRIDE; Q51659; -.
DR EnsemblBacteria; ABL72798; ABL72798; Pden_4737.
DR KEGG; pde:Pden_4737; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_077329_0_0_5; -.
DR OMA; LIDHETC; -.
DR UniPathway; UPA00895; -.
DR Proteomes; UP000000361; Plasmid pPD1222.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004494; MauM_NapG.
DR Pfam; PF12838; Fer4_7; 2.
DR TIGRFAMs; TIGR00397; mauM_napG; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; Plasmid;
KW Reference proteome; Repeat; Signal; Transport.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..224
FT /note="Methylamine utilization ferredoxin-type protein
FT MauM"
FT /id="PRO_0000008847"
FT DOMAIN 54..84
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 91..124
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 133..169
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 177..208
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 224 AA; 23695 MW; F7758CA696293F37 CRC64;
MEARMTGRRK VTRRDAMADA ARAVGVACLG GFSLAALVRT ASPVDARAIR PPGALPEQDF
LAACVHCGLC VQACPYGTLS LAEWSDEAEL GTPFFTPREV PCYMCKDVPC ARACPTGALD
RDIPSIRDAD MGVAVLVGHE TCLNYKGLNC SICVRVCPIR GDAISLEPQE IDGRRVMIPV
VHSASCTGCG TCEKQCVLGH AAIRVLPRDL GLGGPGRNRA GRKA
