ID A1BB99_PARDP Unreviewed; 200 AA.
AC A1BB99;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Methylamine utilization protein MauD {ECO:0000256|ARBA:ARBA00019076};
GN OrderedLocusNames=Pden_4732 {ECO:0000313|EMBL:ABL72793.1};
OS Paracoccus denitrificans (strain Pd 1222).
OG Plasmid pPD1222 {ECO:0000313|Proteomes:UP000000361}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL72793.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RC PLASMID=pPD1222 {ECO:0000313|Proteomes:UP000000361};
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: May be specifically involved in the processing, transport,
CC and/or maturation of the MADH beta-subunit.
CC {ECO:0000256|ARBA:ARBA00003475}.
CC -!- PATHWAY: One-carbon metabolism; methylamine degradation.
CC {ECO:0000256|ARBA:ARBA00004856}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP000491; ABL72793.1; -; Genomic_DNA.
DR RefSeq; WP_011750952.1; NC_008688.1.
DR AlphaFoldDB; A1BB99; -.
DR EnsemblBacteria; ABL72793; ABL72793; Pden_4732.
DR GeneID; 75504090; -.
DR KEGG; pde:Pden_4732; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_091361_0_0_5; -.
DR OrthoDB; 462848at2; -.
DR UniPathway; UPA00895; -.
DR Proteomes; UP000000361; Plasmid pPD1222.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0030416; P:methylamine metabolic process; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR013478; MeN_DH_accessory.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02661; MauD; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:ABL72793.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..183
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 200 AA; 21746 MW; 991715A60B22B172 CRC64;
MTSFLIASNI LLWLAFLGVT VVMLGLMRQV GLLHERSSPM GAMITDHGPD IGDAAPEFEL
PDFFGRPVRI GGAEAQGRQT LLMFTAPSCP VCDKLFPIIK SIGRAEGINV VMISDGAPEE
HRRFLDSHEL GEMRYVVSAE AGMAFQVGKI PYGVLLDGQG IIRAKGLTNT REHLESLLEA
DKTGFASLQQ YMASRKKQAA
//
