ID A0A0Q8QWJ2_9SPHN Unreviewed; 208 AA.
AC A0A0Q8QWJ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Methylamine utilization protein MauD {ECO:0000256|ARBA:ARBA00019076};
GN ORFNames=ASE22_14270 {ECO:0000313|EMBL:KRB90076.1};
OS Sphingomonas sp. Root720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB90076.1, ECO:0000313|Proteomes:UP000051570};
RN [1] {ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB90076.1, ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|EMBL:KRB90076.1,
RC ECO:0000313|Proteomes:UP000051570};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be required for disulfide bond formation in some
CC proteins. {ECO:0000256|ARBA:ARBA00003565}.
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}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRB90076.1}.
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DR EMBL; LMID01000012; KRB90076.1; -; Genomic_DNA.
DR RefSeq; WP_056361548.1; NZ_LMID01000012.1.
DR AlphaFoldDB; A0A0Q8QWJ2; -.
DR STRING; 1736595.ASE22_14270; -.
DR UniPathway; UPA00895; -.
DR Proteomes; UP000051570; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0030416; P:methylamine metabolic process; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR013478; MeN_DH_accessory.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02661; MauD; 1.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:KRB90076.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051570};
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..185
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 208 AA; 22002 MW; 6F47B24C1BAF069D CRC64;
MNEIFLTAFA LQWVVIVAMG LLMLGLFRQV GMLHERLGPV GALTLSGGSR VGEVAPSFDL
PSLTGGDVVV GGAASDGRST LLFFVSPTCP MCKSMLPIVT AIARENADTT RLVFASDGDE
PAQMKMIVQQ KLADHPFVLS TDLGRAHGVG KLPYAVLLGP DGTVASKGLV NNREHVESLF
EAQRTGIASI QEYAARRDAQ RAHTGAAK
//