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Database: UniProt
Entry: A0A0Q8QWJ2_9SPHN
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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
//
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